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  • 1985-1989  (1,835)
  • 1870-1879
  • 1986  (1,835)
  • Cell & Developmental Biology  (1,316)
  • Biochemistry and Biotechnology  (519)
Source
Material
Years
  • 1985-1989  (1,835)
  • 1870-1879
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Editorial (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 1-1 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060102
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation of cilia from porcine tracheal epithelium and extraction of dynein arms (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 25-34 
    Details
    ISSN: 0886-1544
    Keywords: respiratory cilia ; dynein ; ATPases ; porcine trachea ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Milligram amounts of mammalian ciliary axonemes were isolated from porcine tracheas. These were reactivated upon addition of ATP, indicating intact functional capability with a mean beat frequency at 37°C of 8.2 Hz. Electron microscopy showed typical ultrastructure of the isolated demembranated axonemes. Electrophoresis into polyacrylamide gradient gels containing sodium dodecyl sulfate revealed reproducible protein profiles from ten different tracheal preparations. Four major protein bands were observed in the 300-330 K molecular weight region, as well as tubulin at 51-54K. Extraction of the isolated tracheal axonemes with 0.6M KCl removed the outer dynein arms seen in electron microscopic cross-section of axonemes, preferentially solubilized two of the high molecular weight proteins at 320 and 330 K, and resulted in a three- to four-fold increase in ATPase specific activity. Sedimentation of the dialyzed salt extract on a 5-30% sucrose density gradient and subsequent fractionation yielded two peaks of ATPase activity. The faster migrating, 19S major ATPase peak correlated with the 320 and 330 K proteins, and two other proteins at 81 and 67 K. The slower sedimenting, 12S minor ATPase peak corresponded to a 308 K protein and two smaller proteins at 33 and 48 K. Thus, the outer dynein arm of tracheal cilia appeared to be associated with at least two high molecular weight proteins. These results demonstrate that adequate quantities of functionally intact axonemes can be reproducibly isolated from porcine tracheas, allowing further fractionation and analysis of mammalian cilia.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060105
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  • 3
    Electronic Resource
    Electronic Resource
    Masthead (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060301
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  • 4
    Electronic Resource
    Electronic Resource
    Prelimlnary report on the ultrastructural organization of the contractile appendix of Tontonia appendiculariformis (ciliophora oligotrichina) (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 217-224 
    Details
    ISSN: 0886-1544
    Keywords: contractile system ; microfilaments ; microtubules ; endoplasmic reticulum ; ciliophora ; oligotrichina ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Tontonia appendiculariformis is a marine planktonic ciliate with a long tail. The tail can contract rapidly, becoming transformed into an oval mass one-twentieth of its original length. The highly complex ulrastructure of the tail is described here in detail. A large part of the volume of the tail contains numerous more or less parallel membranous tubes. The membrane of the tubes has numerous invaginations and is probably derived from the smooth endoplasmic reticulum. This tubular material forms a continuous layer around the tail, interrupted in only one region, which contains cilia. Associated with the cilia are basal fibres with a periodically banded appearance. The tubular layer forms several folds separated by hyaloplasm containing many mitochondria. The pellicle of the tail is thrown into numerous pleats. It comprises a perilemma, a plasmalemma, and complex alveoli, but epiplasm and microtubules are absent. The alveoli appear to form septa within the folds of the layer of membranous tubes. In the region where the tail is attached to the body of the ciliate there are conspicuous bundles of microtubules and microfilaments. The membranous tubes and septa appear to be connected to small bundles of microfilaments, which presumably represent the contractile material. However, we consider the membranous tubes as potentially active in producing the change in shape. Although the structure of the tail of Tontonia is unique, there are certain similarities to the stalk of the Tintinnina and also to the motile extension of the dinoflagellate Erythropsidinium.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060221
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  • 5
    Electronic Resource
    Electronic Resource
    Robert Day Allen (1927-1986): An appreciation (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 249-255 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060302
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  • 6
    Electronic Resource
    Electronic Resource
    A model for the molecular basis of filament contractility and sliding as demonstrated by helix models (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 229-236 
    Details
    ISSN: 0886-1544
    Keywords: α-helix ; filament motility ; filament contractility ; filament sliding ; microtubules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The twisting behavior of α helices has hardly been considered hitherto with regard to the function of proteins. The well-known electrostatic repulsion between the highly charged side chains, which depends on their interaction with ions, is absolutely connected with torsional rotations of the helix as long as its hydrogen bonds hold. This means a direct transformation of chemical into mechanical energy. However, the stability of a twisted single α helix with charged side chains is low in an aqueous environment. It may easily ball up to form a globular molecule with nonhelical regions of the polypeptide chain. This corresponds to a primitive contraction that obviously occurs with spasminlike proteins that contain strongly twisted filaments as Salisbury [J. Submicrosc. Cytol. 15:105-110, 1983] has shown. Steps that increase the stability and rigidity of α helical filaments are (1) the formation of coiled-coils, (2) self-intertwining (“telephone cord phenomenon”) or intertwining with other coiled-coils as shown with the intermediate filaments, and (3) association with cytoskeletal elements (microfilaments, protofilaments of microtubules) that contain globular subunits. These coarser elements are rotated by winding and unwinding of the smaller helical molecules and thus transmit the torsion produced in the α helices to the microscopic level by the sliding (screwing) motion and the shearing effect that is connected with the waves of a rotating helix. Particles are transported if connected to the helical side arms. Since the displacement of the side arms seems to occur along the single protofilaments of a microtubule, a rotation of these protofiiaments is suggested. The bidirectional transport of particles along single microtubules may be explained by the association of left- and right-handed helices with the protofilaments. According to the models, parallel and antiparallel sliding of neurofilaments and neurotubules is suggested.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060223
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  • 7
    Electronic Resource
    Electronic Resource
    Regulation of ciliary motility by membrane potential in Paramecium: A role for cyclic AMP (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 256-272 
    Details
    ISSN: 0886-1544
    Keywords: ciliary motility ; cAMP regulation ; swimming speed ; membrane potential ; detergent models ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The membrane potential of Paramecium controls the frequency and direction of the ciliary beat, thus determining the cell's swimming behavior. Stimuli that hyperpolarize the membrane potential increase the ciliary beat frequency and therefore increase forward swimming speed. We have observed that (1) drugs that elevate intracellular cyclic AMP increased swimming speed 2-3-fold, (2) hyperpolarizing the membrane potential by manipulation of extracellular cations (e.g., K+) induced both a transient increase in, and a higher sustained level of cyclic AMP compared to the control, and (3) the swimming speed of detergent-permeabilized cells in MgATP was stimulated 2-fold by the addition of cyclic AMP. Our results suggest that the membrane potential can regulate intracellular cAMP in Paramecium and that control of swimming speed by membrane potential may in part be mediated by cAMP.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060303
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  • 8
    Electronic Resource
    Electronic Resource
    The lack of interaction between vinculin and actin (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 48-55 
    Details
    ISSN: 0886-1544
    Keywords: vinculin ; actin ; adhesion plaques ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Vinculin was purified from chicken gizzard by a modification of the method of Feramisco and Burridge [1980; J Biol Chem 255:1194]. Vinculin did not alter the viscosity of actin as measured in an Ostwald viscometer, nor did it affect actin polymerization as measured with the fluorescent NBD-actin assay. Sedimentation experiments demonstrated that vinculin did not bind to actin, and electron microscopy of negatively stained specimens indicated that vinculin did not aggregate actin filaments into bundles. These results suggest that vinculin, by itself, does not interact with actin at least under commonly used conditions to assay actin-protein interactions in vitro.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060107
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  • 9
    Electronic Resource
    Electronic Resource
    Fungal nuclear behavior analysed by ultraviolet microbeam irradiation (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 35-47 
    Details
    ISSN: 0886-1544
    Keywords: microbeam ; microtubules ; nucleus ; cytoskeleton ; motility ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: During hyphal tip growth in the fungus Basidiobolus magnus, nuclei normally maintain a constant distance from the advancing cell apex by continuously migrating forward. It is not known whether the mechanism that produces nuclear movement also mediates nuclear positioning, or whether these two processes are under separate control. By irradiating small cytoplasmic regions with an ultraviolet microbeam, the coordination between movement and positioning could be disrupted. Regardless of the distance of the target from the nucleus, anterior irradiations (those ahead of the nucleus) caused the nucleus to stop or move backwards, whereas posterior (behind the nucleus) irradiations caused an acceleration in the nuclear velocity. The nucleus retained its ability to move following irradiation, so there was only loss of control over normal positioning. These results suggest that movement and positioning are mediated by different mechanisms. Quantitative microtubule analysis demonstrated that microtubules in the target region had been depolymerized, but in other regions of the cell they were apparently normal. We suggest that the depolymerization of microtubules affects nuclear movement by altering the tensile strength of the cytoplasm, and that cytoskeletal tension mediate nuclear positioning.We also found that accelerated nuclear movement could occur when most of the microtubules surrounding the nucleus were depolymerized. A comparison of the microtubule population surrounding the nucleus in unirradiated versus irradiated cells suggested that microtubules move with nuclei. Therefore, the nucleus does not appear to move via a direct interaction with microtubules.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060106
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  • 10
    Electronic Resource
    Electronic Resource
    Evidence for regulation of lamellipodial and tail contraction of glycerinated chicken embryonic fibroblasts by myosin light chain kinase (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 640-648 
    Details
    ISSN: 0886-1544
    Keywords: cell model ; lamellipodia ; phosphorylation ; Ca2+-dependent contraction ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Permeabilized cell models of muscle and nonmuscle cells have proven useful for examining the regulation of actin, myosin, and other cytoskeletal proteins during cell contraction. Upon addition of Ca2+ and ATP, glycerinated chick embryonic skin fibroblasts retract their tails and lamellipodia. Ca2+-independent contractions are obtained by preincubation of cell models in Ca2+ ATPγS, followed by EGTA and ATP addition, or by addition of trypsin-treated myosin light chain kinase that no longer requires Ca2+ for reactivation. By pretreating cells before glycerination with colchicine, it is possible to study lamellipodial contraction independent of tail contraction. Similar responses to ATPγS pretreatment and unregulated myosin light chain kinase are observed in cells that only contain lamellipodia. SDS-PAGE electrophoresis of glycerinated fibroblasts incubated in ATPγ35S and Ca2+ shows that only two major proteins are thiophosphorylated, and that one of them, a band that comigrates with the 20K MW light chain of myosin, is thiophosphorylated in a Ca2+-dependent manner. Since the rate of tail contraction is several-fold faster after Ca2+ and ATPγS pretreatment or incubation in excess myosin light chain kinase, myosin light chain phosphorylation may be a rate-limiting step during contraction.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060612
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  • 11
    Electronic Resource
    Electronic Resource
    The use of submicroscopic gold particles combined with video contrast enhancement as a simple molecular probe for the living cell (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 105-113 
    Details
    ISSN: 0886-1544
    Keywords: video-microscopy ; colloidal gold ; immunocytochemistry ; microtubules ; receptors ; saltatory motion ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We describe a new approach to probe the molecular biology of the living cell that uses small colloidal gold particles coupled to specific ligands. They are visualized in cells by bright-field, video enhanced contrast microscopy. We describe the basic aspects of the technique and provide examples of applications to intracellular motility, cell membrane dynamics, receptor translocation, internalization, and intracellular routing. We also provide examples of the use of this approach in immunospecific labelling of cells and tissue sections.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060207
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  • 12
    Electronic Resource
    Electronic Resource
    Incorporation and turnover of labeled exogenous tubulin in the mitotic spindles of Chaetopterus oocytes and HeLa cells (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 114-121 
    Details
    ISSN: 0886-1544
    Keywords: mitosis ; microtubules ; tubulin incorporation ; assembly polarity ; Chaetopterus ; HeLa cells ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The incorporation of tubulin into mitotic spindles in situ was studied by incubating permeabilized mitotic cells in solutions containing [3H]GTP-labeled or dichlorotriazinylamino fluorescein (DTAF)-labeled tubulin. Metaphase HeLa cells or spindle-containing “minicells” from Chaetopterus oocytes were lysed in a microtubule-assembly buffer plus 0.5% Nonidet P-40, 1 mg/ml 120,000g supernatant mammalian brain tubulin, and [3H]GTP. After different periods of incubation, mitotic spindles were isolated in 2 M-glycerol-containing assembly buffer and separated from unbound counts by centrifugation through a 4 M-glycerol cushion; 3H counts per mg protein increase linearly for 8-12 min and then reach a plateau or steady state in both Chaetopterus oocytes and HeLa cells. Addition of 4 mM CaCl2 blocks or reverses incorporation. Little or no [3H]GTP is incorporated if exogenous tubulin or lysed cells are omitted from the assembly mixture.To measure the loss rate of [3H]GTP-tubulin from mitotic spindles, cells were incubated in tubulin plus [3H]GTP for 30 min, and a 20-fold excess of cold GTP (2 mM) was added. Samples were removed after incubation for different periods, and spindles were isolated as described above and counted for 3H content. [3H]GTP is lost from spindles at a rate of about 16%/min until a new steady state is reached in about 8 min. These results are consistent with an incorporation and turnover of [3H]GTP-tubulin in spindle microtubules of these lysed-cell models.The location of this newly incorporated tubulin in the spindle was investigated by incorporating fluorescent DTAF-tubulin into mitotic spindles of these lysed cell types. A short pulse (2-5 min) appears to label microtubules (MTs) near metaphase chromosomes and longer exposures label the entire spindle.The rates of incorporation and turnover that we see by [3H]GTP and fluorescent tubulin incorporation in situ are faster than those observed with brain MTs at steady state in vitro but are in the range of the rates of spindle fiber formation in prophase, and spindle MT reassembly after cooling.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060208
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  • 13
    Electronic Resource
    Electronic Resource
    Towards a new classification of intracellular particle movements based on quantitative analyses (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 128-135 
    Details
    ISSN: 0886-1544
    Keywords: motion analysis ; axonal transport ; cytoplasmic transport ; Brownian motion ; AVEC-DIC microscopy ; saltatory particle motion ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A survey study of organelle movements in a variety of cell types of plant and animal origin was made with the aid of video-enhanced contrast, differential interference contrast (AVEC-DIC) microscopy followed by fine analysis of the motile behavior of the individual organelles. We found that there exists besides Brownian motion a wide spectrum of active motions in cells, i.e. motion that is directionally biased through the expenditure of metabolic energy. The types of active motion seen range from a continuous motion (sometimes appearing as streaming) in plant cells and neurons to various types of less ordered and less well directed motion. We did not see any clear-cut qualitative difference between plant and animal cells or between systems presumed to be actin- and microtubule-based. A preliminary classification of the types of active motion is presented. The ongoing research activities, which aim at a more precise definition of the different types of motion by a set of quantitative parameters, are described, and the progress made so far is reported.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060210
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  • 14
    Electronic Resource
    Electronic Resource
    Polarized cytoplasmic movement and inhibition of saltations induced by calcium-mediated effects of microbeams in fungal hyphae (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 136-145 
    Details
    ISSN: 0886-1544
    Keywords: cytoplasmic movement ; microbeam ; Ca++ ; fungi ; saltatory movement ; cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have investigated the mechanisms that hyphae of the fungus Basidiobolus magnus use to accomplish bulk movement of their cytoplasm and saltatory organelle movements. When cells were irradiated with an ultraviolet microbeam, cytoplasmic contraction occurred. The posterior cytoplasm (toward the septum) always moved forward toward the irradiated area, whereas anterior cytoplasm (between the cell tip and target) never contracted back toward the site of irradiation. Thus, there is an intrinsic polarity in the cytoplasm. Irradiations also arrested saltatory movements. The effects of irradiation on both saltations and cytoplasmic movement appear to be mediated by Ca++. Chelating exogenous Ca++ before irradiation eliminated contractions and prevented the inhibition of saltations. Furthermore, the effects of irradiation could be duplicated by using the Ca++ ionophore A23187. We relate the present results to our previous report on the effects of irradiation on the cytoskeleton [McKerracher and Heath, 1986]. We conclude that two separate cytoskeletal networks exist in fungal cells, and that an actin-containing network generates bulk cytoplasmic movement.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060211
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  • 15
    Electronic Resource
    Electronic Resource
    In vitro movements of actin and myosin filaments from muscle (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 159-162 
    Details
    ISSN: 0886-1544
    Keywords: superprecipitation ; actomyosin ; F-actin bundle ; unidirectional sliding ; sliding velocity ; dark field microscopy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Unidirectional sliding of myosin filaments along F-actin bundles was produced with purified muscle actin and myosin in the presence of ATP. The velocity of myosin filament sliding was independent of myosin filament length. This result supports a recent hypothesis that long distance movement of myosin cross-bridge can be induced by splitting of one ATP molecule [Yanagida, Arata, and Oosawa, 1985. Nature. 316:366-369; Higashi-Fujime. 1985. J. Cell Biol., 101:2335-2344].
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060214
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  • 16
    Electronic Resource
    Electronic Resource
    Structural evidence for contractile units in the giant smooth muscle cell of Beröe (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 153-158 
    Details
    ISSN: 0886-1544
    Keywords: giant smooth muscle fiber ; ctenophore ; myofilaments ; ultrastructure ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Bundles of giant smooth muscle fibers of the ctenophore Beröe have been stretched up to four times their initial length and then examined by transmission electron microscopy. Stretching induces the segregation of actin and thick (myosinlike) filaments into separate domains. The thick filaments domains are made of 20-30 filaments, with a regular spacing identical to that of nonstretched fibers. A moderate stretching permits the visualization of microtendons associating actin filament bundles to hyaluronidase-resistant condensations of the extracellular matrix. It is deduced from these observations that Beröe giant smooth muscle fibers possess myofibrils which attach at both ends upon the sarcolemmal membrane. Each myofibril is probably made of two long actin filament bundles (of approximately 150 filaments) and short (2-3 μm) myosinlike bundles (of approximately 30 filaments).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060213
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  • 17
    Electronic Resource
    Electronic Resource
    Motility and centrosomal organization during sea urchin and mouse fertilization (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 163-175 
    Details
    ISSN: 0886-1544
    Keywords: centrosomes ; fertilization ; mice ; microfilaments ; microtubules ; mitosis ; pericentriolar material ; sea urchins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Motility and the behavior and inheritance of centrosomes are investigated during mouse and sea urchin fertilization. Sperm incorporation in sea urchins requires microfilament activity in both sperm and eggs as tested with Latrunculin A, a novel inhibitor of microfilament assembly. In contrast the mouse spermhead is incorporated in the presence of microfilament inhibitors indicating an absence of microfilament activity at this stage. Pronuclear apposition is arrested by microfilament inhibitors in fertilized mouse oocytes. The migrations of the sperm and egg nuclei during sea urchin fertilization are dependent on microtubules organized into a radial monastral array, the sperm aster. Microtubule activity is also required during pronuclear apposition in the mouse egg, but they are organized by numerous egg cytoplasmic sites. By the use of an autoimmune antibody to centrosomal material, centrosomes are detected in sea urchin sperm but not in unfertilized eggs. The sea urchin centrosome expands and duplicates during first interphase and condenses to form the mitotic poles during division. Remarkably mouse sperm do not appear to have the centrosomal antigen and instead centrosomes are found in the unfertilized oocyte. These results indicate that both microfilaments and microtubules are required for the successful completion of fertilization in both sea urchins and mice, but at different stages. Furthermore they demonstrate that centrosomes are contributed by the sperm during sea urchin fertilization, but they might be maternally inherited in mammals.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060215
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  • 18
    Electronic Resource
    Electronic Resource
    Cell surface displacement during euglenoid movement and its computer simulation (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 186-192 
    Details
    ISSN: 0886-1544
    Keywords: Euglena ; pellicular strip ; cell shape ; sliding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We recently showed by videomicroscopy that adjacent pellicular strips slide relative to each other without contraction during S-shaped bending movement in Euglena fusca (Suzaki and Williamson, 1985). In order to validate this sliding strip mechanism for other species and other shape changes, a theoretical analysis and a computer simulation were carried out. Some of the commonly observed euglenoid cell shapes (rounded. S-shaped, and embryo-like shapes) were generated. Our results suggest that Euglena probably achieves a variety of cell shape changes by means of locally regulated sliding between adjacent pellicular strips of constant length and width.
    Additional Material: 21 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060217
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  • 19
    Electronic Resource
    Electronic Resource
    Masthead (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986) 
    Details
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010101
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  • 20
    Electronic Resource
    Electronic Resource
    Editorial (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 1-1 
    Details
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010102
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  • 21
    Electronic Resource
    Electronic Resource
    Comment: “Dry” enzymes (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 2-3 
    Details
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010103
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    Electronic Resource
    Electronic Resource
    Proteins and peptides in water-restricted environments (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 4-15 
    Details
    ISSN: 0887-3585
    Keywords: membrane biomimetic system ; reverse micelles ; interfacial water ; myelin proteins ; solid enzyme activity ; organic solvents ; biotechnology ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010104
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  • 23
    Electronic Resource
    Electronic Resource
    The design, synthesis, and crystallization of an alpha-helical peptide (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 16-22 
    Details
    ISSN: 0887-3585
    Keywords: protein design ; alpha-helical bundle ; x-ray crystallography ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Twelve- and sixteen-residue peptides have been designed to form tetrameric alphahelical bundles. Both peptides are capable of folding into amphiphilic alpha-helices, with leucyl residues along one face and glutamyl and lysyl residues along the opposite face. Four such amphiphilic alpha-helices are capable of forming a noncovalently bonded tetramer. Neighboring helices run in antiparallel directions in the design, so that the complex has 222 symmetry. In the designed tetramer, the leucyl side chains interdigitate in the center in a hydrophobic interaction, and charged side chains are exposed to the solvent. The designed 12-mer(ALPHA-1) has been synthesized, and it forms helical aggregates in aqueous solution as judged by circular dichroic spectroscopy. It has also been crystallized and characterized by x-ray diffraction. The crystal symmetry is compatible with (but does not prove) the design. The design can be extended to a four-alpha-helical bundle formed from a single polypeptide by adding three peptide linkers.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010105
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  • 24
    Electronic Resource
    Electronic Resource
    The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 23-33 
    Details
    ISSN: 0887-3585
    Keywords: peptide helix ; protein stability ; framework model of folding ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Recent work has shown that, with synthetic analogues of C-peptide (residues 1-13 of ribonuclease A), the stability of the peptide helix in H2O depends strongly on the charge on the N-terminal residue. We have asked whether, in semisynthetic ribonuclease S reconstituted from S-protein plus an analogue of S-peptide (1-15), the stability of the peptide helix is correlated with the Tm of the reconstituted ribonuclease S. Six peptides have been made, which contain Glu9 → Leu, a blocked α-COO- group (—CONH2), and either Gln11 or Glu11. The N-terminal residue has been varied; its charge varies from +2 (Lys) to -1 (succinyl-Ala). We have measured the stability of the peptide helix, the affinity of the peptide for S-protein (by C.D. titration), and the thermal stability of the reconstituted ribonuclease S.All six peptide analogues show strongly enhanced helix formation compared to either S-peptide (1-15) or (1-19), and the helix content increases as the charge on the N-terminal residue changes from +2 to -1. All six peptides show increased affinity for S-protein compared to S-peptide (1-19), and all six reconstituted ribonucleases S show an increase in Tm compared to the protein with S-peptide (1-19). The Tm increases as the charge on residue 1 changes from +2 to -1. The largest increment in Tm is 6°.The results suggest that the stability of a protein can be increased by enhancing the stability of its secondary structure.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010106
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  • 25
    Electronic Resource
    Electronic Resource
    Stabilization of λ repressor against thermal denaturation by site-directed Gly→Ala changes in α-helix 3 (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 43-46 
    Details
    ISSN: 0887-3585
    Keywords: protein stability ; helix-coil ; mutant ; calorimetry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Oligonucleotide-directed mutagenesis has been used to replace α-helical glycines in the N-terminal domain of λ repressor with alanines. Since alanine is a significantly better helix-forming residue than glycine, these changes were predicted to have a stabilizing effect. We show that the Gly46→Ala substitution, the Gly48→Ala substitution, and the double substitution increase the melting temperature of the N-terminal domain by 3-6°.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010108
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  • 26
    Electronic Resource
    Electronic Resource
    Protein folding kinetics by combined use of rapid mixing techniques and NMR observation of individual amide protons (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 34-42 
    Details
    ISSN: 0887-3585
    Keywords: hydrogen exchange ; BPTI ; folding pathway ; protein dynamics ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A method to be used for experimental studies of protein folding introduced by Schmid and Baldwin (J. Mol. Biol. 135: 199-215, 1979), which is based on the competition between amide hydrogen exchange and protein refolding, was extended by using rapid mixing techniques and 1H NMR to provide site-resolved kinetic information on the early phases of protein structure acquisition. In this method, a protonated solution of the unfolded protein is rapidly mixed with a deuterated buffer solution at conditions assuring protein refolding in the mixture. This simultaneously initates the exchange of unprotected amide protons with solvent deuterium and the refolding of protein segments which can protect amide groups from further exchange. After variable reaction times the amide proton exchange is quenched while folding to the native form continues to completion. By using 1H NMR, the extent of exchange at individual amide sites is then measured in the refolded protein. Competition experiments at variable reaction times or variable pH indicate the time at which each amide group is protected in the refolding process. This technique was applied to the basic pancreatic trypsin inhibitor, for which sequence-specific assignments of the amide proton NMR lines had previously been obtained. For eight individual amide protons located in the β-sheet and the C-terminal α-helix of this protein, apparent refolding rates in the range from 15s-1 to 60 s-1 were observed. These rates are on the time scale of the fast folding phase observed with optical probes.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010107
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  • 27
    Electronic Resource
    Electronic Resource
    Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: Effects of ionic strength and amino-acid modification (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 47-59 
    Details
    ISSN: 0887-3585
    Keywords: protein electrostatics ; substrate diffusion ; Poisson-Boltzmann ; electrostatic potentials ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In this paper we report the implementation of a finite-difference algorithm which solves the linearized Poisson-Boltzmann equation for molecules of arbitrary shape and charge distribution and which includes the screening effects of electrolytes. The microcoding of the algorithm on an ST-100 array processor allows us to obtain electrostatic potential maps in and around a protein, including the effects of ionic strength, in about 30 minutes. We have applied the algorithm to a dimer of the protein Cu-Zn superoxide dismutase (SOD) and compared our results to those obtained from uniform dielectric models based on coulombic potentials. We find that both the shape of the protein-solvent boundary and the ionic strength of the solvent have a profound effect on the potentials in the solvent. For the case of SOD, the cluster of positive charge at the bottom of the active site channel produces a strongly enhanced positive potential due to the focusing of field lines in the channel - a result that cannot be obtained with any uniform dielectric model. The remainder of the protein is surrounded by a weak negative potential. The electrostatic potential of the enzyme seems designed to provide a large cross-sectional area for productive collisions. Based on the ionic strength dependence of the size of the positive potential region emanating from the active site and the repulsive negative potential barrier surrounding the protein, we are able to suggest an explanation for the ionic strength dependence of the activity of the native and chemically modified forms of the enzyme.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010109
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  • 28
    Electronic Resource
    Electronic Resource
    A domain of the klenow fragment of Escherichia coli DNA polymerase I has polymerase but no exonuclease activity (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 66-73 
    Details
    ISSN: 0887-3585
    Keywords: protein domain ; polymerase ; 3′-5′ exonuclease ; artificial gene ; expression vector ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The Klenow fragment of DNA polymerase I from Escherichia coli has two enzymatic activities: DNA polymerase and 3′-5′ exonuclease. The crystal structure showed that the fragment is folded into two distinct domains. The smaller domain has a binding site for deoxynucleoside monophosphate and a divalent metal ion that is thought to identify the 3′-5′ exonuclease active site. The larger C-terminal domain contains a deep cleft that is believed to bind duplex DNA. Several lines of evidence suggested that the large domain also contains the polymerase active site. To test this hypothesis, we have cloned the DNA coding for the large domain into an expression system and purified the protein product. We find that the C-terminal domain has polymerase activity (albeit at a lower specific activity than the native Klenow fragment) but no measurable 3′-5′ exonuclease activity. These data are consistent with the hypothesis that each of the three enzymatic activities of DNA polymerase I from E. coli resides on a separate protein structural domain.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010111
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  • 29
    Electronic Resource
    Electronic Resource
    PseqIP: A nonredundant and exhaustive protein sequence data bank generated from 4 major existing collections (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 60-65 
    Details
    ISSN: 0887-3585
    Keywords: computerized data bank ; sequence comparison heuristics ; databank access ; data bank merging ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Four major protein sequence data collections (NBRF-PIR, PSD-Kyoto, PGtrans, and NEWAT) have been merged into a single nonredundant data bank called PseqIP. The data bank entries were automatically matched by a heuristic computer program relying on the fast computation of the number of tetrapeptides shared by two sequences. PseqIP 1.0 includes 6,068 different protein sequences for a total of 1,357,067 residues, representing most of the available sequence information to date. During the course of this work, we found about 600 occurrences course of a protein sequence recorded with a one-amino-acid variation in at least two different data banks. A flat file (ASCII computer-readable format) version of PseqIP 1.0, well-suited for exhaustive homology searches and statistical sequence analysis, is available from our laboratory.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010110
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  • 30
    Electronic Resource
    Electronic Resource
    The galactan-binding immunoglobulin Fab J539: An x-ray diffraction study at 2.6-Å resolution (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 74-80 
    Details
    ISSN: 0887-3585
    Keywords: antibody ; crystal structure ; anti-galactan ; J539 ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The crystal structure of the Fab of the galactan-binding immunoglobulin J539 (a mouse IgA,κ) has been determined at a resolution of approximately 2.6 Å by X-ray diffraction. The starting model was that obtained from the real space search described previously (Navia, M.A., Segal, D.M., Padlan, E.A., Davies, D.R., Rao, D.N., Rudikoff, S. and Potter, M. “Crystal structure of galactan-binding mouse immunoglobulin J539 Fab at 4.5 Å resolution.” Proc. Nat. Acad. Sci. USA, 76:4071-4074, 1979). This Fab structure has now been refined by restrained least-squares procedures to an R-value of 19% for the 11,690 unique reflections between 8.0 Å and 2.6 Å. The rms deviation from ideal bond lengths is 0.025 Å. The overall structure differs from McPC603 Fab, another mouse IgA,κ antibody, in that the elbow bend, relating the variable and constant parts of the molecule, is 145° vs. 133° for McPC603. The region of the molecule expected to be the antigen binding site contains a large cavity with two clefts leading away from it. This has been fitted with a model of an oligo-galactan.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010112
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  • 31
    Electronic Resource
    Electronic Resource
    Reciprocal control of retinal rod cyclic GMP phosphodiesterase by its γ subunit and transducin (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 90-99 
    Details
    ISSN: 0887-3585
    Keywords: visual excitation ; rhodopsin ; enzyme regulation ; cyclic nucleotide cascade ; G-proteins ; inhibitory subunit ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The switching on of the cGMP phosphodiesterase (PDE) in retinal rod outer segments by activated transducin (Tα-GTP) is a key step invisual excitation. The finding that trypsin activates PDE (αβγ) by degrading its γ subunit and the reversal of this activation by γ led to the proposal that Tα-GTP activates PDE by relieving an inhibitory constraint imposed by γ (Hurley and Stryer: J. Biol. Chem. 257:11094-11099, 1982). We report here studies showing that the addition of γ subunit also reverses the activation of PDE by Tα-GTP-γS. A procedure for preparing γ in high yield (50-80%) is presented. Analyses of SDS polyacrylamide gel slices confirmed that inhibitorya activity resides in the γ subunit. Nanomolar γ blocks the activation of PDE by micromolar Tα-GTPγS. The degree of activation of PDE depends reciprocally on the concentrations of γ and Tα-GTPγS. γ remains bound to the disk membrane during the activation of PDE by transducin. The binding of γ to the αβ subunits of native PDE is very tight; the dissociation constant is less than 10 pM, indicating that fewer than 1 in 1,700 PDE molecules in rod outer segments are activated in the absence of Tα-GTP.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010114
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  • 32
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    Electronic Resource
    Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 81-89 
    Details
    ISSN: 0887-3585
    Keywords: protein stability ; protein denaturation ; denatured state ; structural intermediates ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Eleven mutant forms of staphylococcal nuclease with one or more defined amino acid substitutions have been analyzed by solvent denaturation by using intrinsic fluorescence to follow the denaturation reaction. On the basis of patterns observed in the value of m-the rate of change of log Kapp (the apparent equilibrium constant between the native and denatured states) with denaturant concentration - these proteins can be grouped into two classes. For class I mutants, the value of m with guanidine hydrochloride is less than the wild-type value and is either constant or increases slightly with increasing denaturant; the value of m with urea is also less than wild type but shows a marked increase with increasing denaturant concentration, often approaching but never exceeding the wild-type value. For class II mutants, m is constant and is greater than wild type in both denaturants, with the increase being consistently larger in guanidine hydrochloride than in urea. When double or triple mutants are constructed from members of the same mutant class, the change in m is usually the sum of the changes produced by each mutation in isolation. One plausible explanation for these altered patterns of denaturation is that chain-chain or chain-solvent interactions in the denatured state have been modified - interactions which appear to involve hydrophobic groups.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010113
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  • 33
    Electronic Resource
    Electronic Resource
    Masthead (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986) 
    Details
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010201
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  • 34
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    A novel method for selective isolation of C-terminal peptides from tryptic digests of proteins by immobilized anhydrotrypsin: Application to structural analyses of the tail sheath and tube proteins from bacteriophage T4 (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 100-107 
    Details
    ISSN: 0887-3585
    Keywords: affinity chromatography ; high-performance liquid chromatography ; bacteriophage T4 tail sheath protein ; bacteriophage T4 tail tube protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A novel method useful for selective isolation of the C-terminal peptide from a tryptic digestion mixture of a protein has been developed by taking advantage of a unique property of anhydrotrypsin, which has a strong specific affinity for the peptides containing arginine or lysine at their C-termini. Briefly, peptides produced by tryptic digestion of a protein are fractionated by affinity chromatography on a column of immobilized anhydrotrypsin. The C-terminal peptide is recovered in a breakthrough fraction, which the remainders are adsorbed on the column (unless the protein ends in arginine or lysine). The breakthrough fraction is then subjected to reversed-phase high-perfomance liquid chromatography in order to purify the C-terminal peptide. Using this method, we have successfully isolated the C-terminal peptides from tryptic digests of the sheath protein (gp 18) and the tube protein (gp 19) of bacteriophage T4. The analytical results on these peptides, together with the information on the N-terminal structures of the original proteins and on the nucleotide sequences of genes 18 and 19, allowed us to establish the complete primary structures of the two proteins.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010115
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  • 35
    Electronic Resource
    Electronic Resource
    Protein fluorescence quenching by small molecules: Protein penetration versus solvent exposure (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 109-115 
    Details
    ISSN: 0887-3585
    Keywords: proteins ; protein dynamics ; tryptophan exposure ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Experiments were done to test the thesis that acrylamide and similar small molecules can penetrate into proteins on a nanosecond time scale. The approach taken was to measure the pattern of fluorescence quenching exhibited by quenching molecules differing in molecular character (size, polarity, charge) when these are directed against protein tryptophans that cover the whole range of tryptophan accesibility. If quenching involves protein penetration and internal quencher migration, one expects that larger quenchers and more polar quenchers should display lesser quenching. In fact, no significant dependence on quencher character was found. For proteins that display measurable quenching, the disparate quenchers studied display very similar quenching rate constants when directed against any particular protein tryptophan. For several proteins having tryptophans known to be buried, no quenching occurs. These results are not consistent with the view that the kinds of small molecules studied can quite generally penetrate into and diffuse about within proteins at near-diffusion-limited rates. Rather the results suggest that when quenching is observed, the pathway involves encounters with tryptophans that are partially exposed at the protein surface. Available crystallographic results support this conclusion.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010202
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  • 36
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    Translational repression in vitro by the bacteriophage T4 regA protein (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 116-124 
    Details
    ISSN: 0887-3585
    Keywords: translational repressor ; in vitro transcription-translation ; gene expression ; protein purification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The bacteriophage T4 translational represor regA protein has been purified from an overproducing strain, and its activity has been studied in simple in vitro protein synthesis reactions. RegA protein was found to inhibit the translation of T4 genes 44, 45, and ORF45-1 in a concentration-dependent fashion. Expression of two other T4 genes which are insensitive to regA protein in vivo, genes 32 and 43, was unaffected by the presence of regA protein. Specific inhibition of synthesis of genes 44, 45, and ORF 45-1 proteins was achieved with 5-20 μM concentrations of regA protein, without the addition of any other T4 encoded proteins or cofactors. When in vitro protein synthesis was performed in two steps, uncoupling translation from transcription, regA protein had an inhibitory effect regardless of whether it was added at the initiation of transcription or only at the translation step. This indicates that regA protein functions during the translation step of protein synthesis in vitro in agreement with previous in vivo studies of regA protein.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010203
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  • 37
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    Cloning, expression, and nucleotide sequence of livR, the repressor for high-affinity branched-chain amino acid transport in Escherichia coli (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 125-133 
    Details
    ISSN: 0887-3585
    Keywords: regulation ; prokaryotic bacteria ; leucine uptake ; leucyl tRNA corepressor ; cell physiology ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The livR gene encoding the repressor for high-affinity branched-chain amino acid transport in Escherichia coli has been cloned from a library prepared from the episome F106. The inserted DNA fragment from the initial cloned plasmid, pANT1, complemented two independent, spontaneously derived, regulatory mutations. Subcloning as well as the creation of deletions with Bal31 exonuclease revealed that the entire regulatory region is contained within a 1.1-kb RsaI-SalI fragment. Expression of the pANT plasmids in E. coli minicells showed that the regulatory region encodes one detectable protein with an apparent molecular weight of 21,000. DNA sequencing revealed one open reading frame of 501 bp encoding a protein with a calculated MW of 19,155. The potential secondary structure of the regulatory protein has been predicted and it suggests that the carboxy terminus may fold into three consecutive alpha helices. These results suggests that the livR gene encodes a repressor which plays a role in the regulation of expression of the livJ and the livK transport genes.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010204
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  • 38
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    Peptide and ester synthesis in organic solvents catalyzed by seryl proteases linked to alumina (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 134-138 
    Details
    ISSN: 0887-3585
    Keywords: enzymatic transesterification ; peptide synthesis ; trypsin ; chymotrypsin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Trypsin and α-chymotrypsin were immobilized to alumina-phosphocolamine complex, activated by glutaraldehyde. The immobilized enzymes show a great stability toward organic solvents miscible or immiscible with water. In the presence of a low concentration of water, the immobilized enzymes catalyzed transesterification reactions as well as peptide synthesis. The synthesized peptides were stable toward the immobilized enzymes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010205
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  • 39
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    Isolation and characterization of native human renin derived from Chinese hamster ovary cells (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 139-145 
    Details
    ISSN: 0887-3585
    Keywords: hypertension ; renin production ; mammalian expression ; affinity chromatography ; genetic engineering ; prorenin secretion ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Transfection of Chinese hamster ovary (CHO) cells with a plasmid containing the cDNA for human preprorenin has provided cell lines that secrete 15 mg of native prorenin per liter of culture medium. Tryptic activation of the prorenin occurs by selective cleavage of the Arg66-Leu67 bond (numbering as in preprorenin). The renin product, purified in a single step and in high yield by affinity chromatography, is fully stable for as long as 8 months when stored in solution at 4°C and pH 6.5. Purity of the renin was judged to be greater than 95% by gel electrophoresis, compositional and N-terminal sequence analyses, and specific enzyme activity. An important aspect of the present work is the development of a direct assay for renin which permits accurate and reproducible evaluation of enzyme units and kinetic parameters. Application of methods described herein, combined with appropriate scale-up fermentation capabilities, provides the means for generating gram quantities of human renin and its zymogen.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010206
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  • 40
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    An algorithm for determining the conformation of polypeptide segments in proteins by systematic search (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 146-163 
    Details
    ISSN: 0887-3585
    Keywords: protein conformation ; energy calculations ; protein modeling ; loop conformation ; surface area ; homologous proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The feasibility of determining the conformation of segments of polypeptide chain up to six residues in length in globular proteins by means of systematic search through the possibles conformations has been investigated. Trial conformations are generated by using representative sets of φ, ψ, and χ angels that have been derived from an examination of the distributions of these angles in refined protein structures. A set of filters based on simple rules that protein structures obey is used to reduce the number of conformations to a manageable total. The most important filters are the maintenance of chain integrity and the avoidance of tooshort van der Waals contacts with the rest of the protein and with other portions of the segment under construction. The procedure is intended to be used with approximate models so that allowance is made throughout for errors in the rest of the structure. All possible main chains are first constructed and then all possible side-chain conformations are built onto each of these. The electrostatic energy, including a solvent screening term, and the exposed hyrophobic area are evaluated for each accepted conformation. The method has been tested on two segments of chain in the trypsin like enzyme from Streptomyces griseus. It is found that there is a wide spread of energies among the accepted conformations, and the lowest energy ones have satisfactorily small root mean square deviations from the X-ray structure.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010207
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    pH Dependence of 2,3-diphosphoglycerate binding to human hemoglobin Ao at 21.5°C (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 164-175 
    Details
    ISSN: 0887-3585
    Keywords: DPG ; organophosphates ; ligand interactions ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Rate equilibrium dialysis was used to measure the binding of 2,3-diphosphoglycerate (DPG) to human oxy- and deoxyhemoglobin AO over the range pH 5-9, at 21.5°C. This approach yielded an accurate, precise, and self-consistent set of model-independent association constants. These data were successfully fitted to a thermodynamic model which is fuctionally similar to a Hill equation. The isotherms generated by this fitting procedure appear to intersect at low pH and converge at high pH. This apparent convergence at high pH is consistent with results obtained by oxygen equilibria studies performed under conditions of saturating DPG. These calculated isotherms were used to determine the enhancement of the Bohr effect as a function of pH. These results are consistent with data obtained by pH stat measurements by other investigators.This paper presents the first in a series of studies that will provide a systematic characterization of the interaction between hemoglobin and DPG.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010208
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    The restoration of electron micrographs blurred by drift and rotation (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 176-187 
    Details
    ISSN: 0887-3585
    Keywords: drifted micrographs ; rotational blur ; thin sections ; Wiener filtering ; image analysis ; sickle hemoglobin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: We have investigated the restoration of electron micrographs exhibiting blurring due to drift and rotation. Blurring due to drift arises in micrographs taken of a specimen which is moving relative to the image plane. A related problem is that of rotational blurring which arises in micrographs of thin sections of helical particles viewed in cross section. The twist of the particle within the finite thickness of the section causes the image to appear rotationally blurred about the helical axis.Restoration algorithms were evaluated by applying them to the restoration of blurred model images degraded by additive Gaussian noise. Model images were also used to investigate how an incorrect estimate of the point spread function function describing the blur would effect the restoration. Images were, if necessary, geometrically transformed to a space in which the point spread function of the blur can be considered as linear and space invariant as, under these conditions, the restoration algorithms are greatly simplified. In the case of the rotationally blurred images this procedur was accomplished by transforming the image to polar coordinates.The restoration techniques were successfully applied to blurred micrographs of bacteriophage T4 and crystals of catalase. The quality of the restoration was judged by comparisons of the restored images to undegraded images. Application to micrographs of rotationally blurred cross sections of helical macrofibers of sickle hemoglobin resulted in a reduction in the amount of rotational blurring.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010209
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    Activation of retinal rod cyclic GMP-phosphodiesterase by transducin: Characterization of the complex formed by phosphodiesterase inhibitor and transducin α-subunit (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 188-193 
    Details
    ISSN: 0887-3585
    Keywords: G-protein ; phototransduction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The GTP-binding subunit of transducin (Tα) activates the cGMP phosphodiesterase (PDE) of bovine retinal rods by relieving the constraint imposed by the inhibitory subunit PDEγ. We have isolated and characterized the complex Tα.GTPγS-PDEγ formed when Tα is activated by the nonhydrolyzable analog GTPγS. Sedimentation and light-scattering techniques demonstrate that, in contrast to free Tγ.GTPγS, which is soluble, the Tα.GTPγS-PDEγ complex, as well as Tα.GTP-PDEγ, is membrane bound at cytosolic ionic strength. It is eluted from the membrane at low ionic strength as a monomeric and 1:1 stoichiometric complex. The relative affinities of PDEγ for PDEαβ and for Tα.GTP are discussed.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010210
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    Electronic Resource
    Masthead (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986) 
    Details
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010301
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  • 45
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    Set of novel, conserved proteins fold pre-messenger RNA into ribonucleosomes (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 195-210 
    Details
    ISSN: 0887-3585
    Keywords: protein domains ; oligomeric assembly ; RNA splicing ; multiple binding sites ; RNP core proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 2 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010302
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    Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 211-217 
    Details
    ISSN: 0887-3585
    Keywords: protein folding ; α-helix stabilization ; peptide structural stability ; circular dichroism ; protein electrostatics ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The effects of trifluoroethanol (TFE) on the stability of the α-helix formed by ribonuclease S-peptide, residues 1-19 of ribonuclease A, were studied by measuring circular dichroism as a function of TFE concentration, pH, and temperature. The S-peptide forms an unusually stable α-helix, which is known to be stabilized by TFE. The magnitude of the effect of charged groups on the peptide, manifested by the change in α-helix stability as a function of pH, was not altered significantly by either TFE concentration or temperature, indicating that the lower dielectric constant of TFE is not important in the stabilization of this α-helix. This suggests that the α-helix might be stabilized by many interactions in addition to the effects of charges. The titration curve of circular dichroism vs. TFE concentration appears to be cooperative at 0°C, but becomes progressively less cooperative at temperatures between 25 and 75°C. The properties of the TFE stabilization indicate that TFE might be a useful probe with which to measure the stability of marginally stable peptides and small proteins.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010303
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  • 47
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    The DNA replication inhibitor microcin B17 is a forty-three-amino-acid protein containing sixty percent glycine (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 230-238 
    Details
    ISSN: 0887-3585
    Keywords: microcins ; peptide antibiotic ; protein processing ; HPLC ; protein secretion ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Microcin B17 is a low-molecular-weight protein that inhibits DNA replication in a number of enteric bacteria. It is produced by bacterial strains which harbor a 70-kilobase plasmid called pMccB17. Four plasmid genes (named mcbABCD) are required for its production. The product of the mcbA gene was identified by labelling minicells. The mcbA gene product was slightly larger when a mutation in any of the other three production genes was present. This indicates that these genes are involved in processing the primary mcbA product to yield the active molecule. The mcbA gene product predicted from the nucleotide sequence has 69 amino acids including 28 glycine residues. Microcin B17 was extracted from the cells by boiling in 100 mM acetic acid, 1 mM EDTA, and purified to homogeneity in a single step by high-performance liquid chromatography through a C18 column. The N-terminal amino acid sequence and amino acid composition demonstrated that mcbA is the structural gene for microcin B17. The active molecule is a processed product lacking the first 26 N-terminal residues. The 43 remaining residues include 26 glycines. While microcin B17 is an exported protein, the cleaved N-terminal peptide does not have the characteristic properties of a “signal sequence,” which suggests that it is secreted by a mechanism different from that used by most secreted proteins of E. coli.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010305
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    Properties of a second sensory receptor protein in Halobacterium halobium phototaxis (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 239-246 
    Details
    ISSN: 0887-3585
    Keywords: halobacteria ; photosensory receptor ; retinal ; slow-cycling rhodopsins ; sensory rhodopsins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A second slow-cycling retinylidene protein, in addition to slow-cycling (sensory) rhodopsin (SR), can be bleached with hydroxylamine and regenerated with all-trans retinal in photosensory signaling Halobacterium halobium membranes. Flash photolysis shows this protein undergoes a photochemical reaction cycle characterized by photoconversion of its ground state (λmax 480 nm) to a species with λmax ≤ 360 nm, which thermally regenerates the 480-nm species with a t½ of 260 msec at 25°C, under conditions in which SR photocycles at 650 msec in the same membranes. Mutants characterized with respect to their phototaxis behavior are identified which contain SR and the 480-nm pigment, the latter ranging from undetectable to a concentration equal to that of SR. Receptor mutants lacking all phototaxis sensitivity lack both of the photochemically reactive proteins. The mutant properties contribute to an accumulation of behavioral and spectroscopic evidence that the 480-nm pigment is a second sensory photoreceptor in H. halobium. NaDodSO4-polyacrylamide gel electrophoresis of [3H]retinal-labeled membrane proteins from the mutants indicates SR and the 480-nm pigment contain distinct chromophoric polypeptides differing in their migration rates. The data implicate polypeptides of 25,000 Mr and 23,000 Mr as retinal-binding polypeptides of SR and the 480-nm protein, respectively.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010306
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    A very short peptide makes a voltage-dependent ion channel: The critical length of the channel domain of colicin E1 (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 218-229 
    Details
    ISSN: 0887-3585
    Keywords: colicin E1 ; site-directed mutagenesis ; ion channel ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Cleavage of colicin E1 molecules with a variety of proteases or with cyanogen bromide (CNBr) generates COOH-terminal fragments which have channel-forming activity similar to that of intact colicin in planar lipid bilayer membranes. The smallest channel-forming fragment obtained by CNBr cleavage of the wild-type molecule consists of the C-terminal 152 amino acids. By the use of oligonucleotide-directed mutagenesis, we have made nine mutants along this 152 amino acid peptide, in which an amino acid was replaced by methionine in order to create a new CNBr cleavage site. The smallest of the CNBr-cleaved C-terminal fragments with channel-forming activity, in planar bilayer membranes, was generated by cleavage at new Met position 428 and has 94 amino acids, whereas a 75 amino acid peptide produced by cleavage of a new Met at position 447 did not have channel activity. The NH2-terminus of the channel-forming domain of colicin E1 appears therfore to lie between residues 428 and 447. Since, however, the last six C-terminal residues of the colicin can be removed without changing activity, the number of amino acids necessary to form the channel is 88 or less. In addition, the unique Cys residue in colicin E1 was replaced by Gly, and nine mutants were then made with Cys placed at sequential locations along the peptide for eventual use as sulfhydryl attachment sites to determine the local environment of the replaced amino acid. In the course of making 21 mutants, eight charged residues have been replaced by uncharged Met or Cys without changing the biological activity of the intact molecule.It has been proposed previously that the conformation of the colicin E1 channel is a barrel formed from five or six α-helices, each having 20 amino acids spanning the membrane and two to four residues making the turn at the boundary of the membrane. Our finding that 88 amino acids can make an active channel, combined with recently reported stoichiometric evidence that the channel is a monomer excludes this model and adds significant constraints which can be used in building a molecular model of the channel.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010304
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  • 50
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    Kinetic characterization of early intermediates in the folding of E. coli tryptophan-synthase β2 subunit (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 247-255 
    Details
    ISSN: 0887-3585
    Keywords: protein folding ; domain interactions ; fluorescence transfer ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: This report describes the use of fluorescence energy transfer between an intrinsic energy donor (tryptophan 177) and two chemically added acceptors to study intermediates in the folding of the β2 subunit of E. coli tryptophan-synthase. Two early folding steps are thus identified and characterized. One is very rapid (its rate constant at 12°C is 0.02 sec-1) and corresponds to the folding of the N-terminal domain into a structure whose overall features approximate well those of the native domain. The second step is somewhat slower (its rate constant at 12°C is 0.008 sec-1) and involves a conformational rearrangement of the N-terminal domain brought about by the interactions between the N-and C-terminal domains within a monomeric β chain. This brings to five the number of intermediates which have been identified and ordered on the folding pathway of the dimeric β2 subunit.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010307
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    Preliminary x-ray diffraction analysis of HhaII endonuclease-DNA cocrystals (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 263-266 
    Details
    ISSN: 0887-3585
    Keywords: protein-DNA interaction ; overproducer clone ; sequence-specific recognition ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: HhaII restriction endonuclease purified from an overproducing recombinant E. coli clone has been cocrystallized with a heptanucleotide duplex, d-GGAGTCC:GGACTCC. The cocrystals are monoclonic and belong to the space group C2. The unit cell dimensions are a = 199.0±1.0 Å, b = 100.0±0.5 Å, c = 80.3±0.4 Å, and β = 101.0±1.0°. There appear to be two dimers per asymmetric unit and the crystals diffract to 4-Å resolution.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010309
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    Calculating three-dimensional changes in protein structure due to amino-acid substitutions: The variable region of immunoglobulins (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 267-279 
    Details
    ISSN: 0887-3585
    Keywords: molecular model building ; energy minimization ; homology modeling ; site-specific mutagenesis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A procedure (coupled perturbation procedure, CPP) is introduced as a specific method for calculating the detailed three-dimensional structure of a protein molecule which has a nummber of amino-acid substitutions relative to some previously determined “parent” protein structure. The accuracy of the procedure is tested by calculating the conformation of a region of the human immunoglobulin fragment Fab Kol based on the analogous region of the human immunoglobulin fragment Fab New. Both structures have previously been determined crystallographically. The calculated model is accurate to the extent that both of the sequence differences in the region are modeled correctly and that conformational changes in a number of nearby residues are correctly identified. CPP is shown to give better results than other commonly used modeling procedures when applied to the same problem.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010310
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    Proteolytic dissection of a hapten binding site (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 256-262 
    Details
    ISSN: 0887-3585
    Keywords: FV fragment ; space filling hapten ; reconstitution ; scratched analysis ; equilibrium dialysis ; contact residues ; hypervariable loops ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: IgG Gar, a human myeloma protein that binds riboflavin with a high affinity, was used to derive variable region fragments from the heavy chain and the light chain. Riboflavin binding ability of the active site generated by V(H) and light chain and the active site generated by V(H) and V(L) was compared to riboflavin binding by the F(ab) fragment. The riboflavin binding ability of the F(ab) fragment is the same as the intact molecule, while the binding ability of the active site formed by V(H) and light chain is lowered by two to three orders of magnitude, indicating that the removal of C(H1) domain decreases the interaction between riboflavin and the amino acids that is important in tight binding of riboflavin. Removal of the third hypervariable region and the constant region domain from the light chain further lowers the binding constant by one order of magnitude. The results indicate that the V(H) and V(L) segments of IgG Gar can reconstitute a riboflavin binding site. The decrease in affinity probably reflects a decrease in the rigidity with which the hypervariable loops are held together to place the contact amino acid residues in optimal contact with the hapten.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010308
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    Affinity of nonhomologous amphiphilic peptides toward a monoclonal antibody raised against apolipoprotein A-I (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 280-286 
    Details
    ISSN: 0887-3585
    Keywords: antibody affinity ; ELISA ; β-endorphin models ; melittin model ; amphiphilic α-helix ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Monoclonal antibodies against human apolipoprotein A-I (apoA-I) were generated by the hybridoma technique. Clone G-10 was selected on the basis of its highest titer. The affinity of this antibody toward a series of synthetic peptides differing in length, amino acid composition, and amphiphilicity was tested by using both the indirect and the competitive enzyme-linked immunosorbent techniques (ELISA). From these measurements we calculated dissociation constants of the complexes of the antibody with apoA-I bound to the surface of the microtiter plate, apoA-I in solution, and any of the several peptides in solution. The dissociation constant (Kd) of the immobilized apoA-I/anti-apoA-I-complex, Kd = 2 × 10-9 M, was significantly lower than that of the complex resulting from the interaction between anti-apoA-I and either apoA-I in solution or any of the several amphiphilic helical peptides in solution. Peptides devoid of amphiphilic secondary structure were inert. These data are consistent with the proposal that monoclonal G-10 recognizes in antigenic peptides an α-helical secondary structure of defined hydrophilic-lipophilic balance and comparatively less the specific amino acid side chains. We propose that the highest contribution to the free energy of binding (8 Kcal/mole) is derived from the docking of the helix to the antibody. It follows that in probing the specificity of a monoclonal antibody the conformation and the physical environment of the interacting antigen must be taken into account.
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    URL: http://dx.doi.org/10.1002/prot.340010311
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    Electronic Resource
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    Masthead (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986) 
    Details
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010401
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    Editorial (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. i 
    Details
    ISSN: 0887-3585
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010402
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  • 57
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    Isolation and analysis of arc repressor mutants: Evidence for an unusual mechanism of DNA binding (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 302-311 
    Details
    ISSN: 0887-3585
    Keywords: mutant proteins ; protein stability ; operator binding ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: We have isolated 64 different missense mutations at 36 out of 53 residue positions in the Arc repressor of bacteriophage P22. Many of the mutant proteins with substitutions in the C-terminal 40 residues of Arc have reduced intracellular levels and probably have altered structures or stabilities. Mutations in the N-terminal ten residues of Arc cause large decreases in operator DNA binding affinity without affecting the ability of Arc to fold into a stable three-dimensional structure. We argue that these N-terminal residues are important for operator recognition but that they are not part of a conventional helix-turn-helix DNA binding structure. These results suggest that Arc may use a new mechanism for sequence specific DNA binding.
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    URL: http://dx.doi.org/10.1002/prot.340010404
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    Molecular structure and evolution of adrenergic and cholinergic receptors (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 287-301 
    Details
    ISSN: 0887-3585
    Keywords: primary sequence homology ; primary structure ; secondary structure ; quaternary structure ; gene cloning ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340010403
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    Primary structure of the reaction center from Rhodopseudomonas sphaeroides (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 312-325 
    Details
    ISSN: 0887-3585
    Keywords: membrane proteins ; nucleotide sequence ; evolution ; photosynthesis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The reaction center is a pigmentprotein complex that mediates the initial photochemical steps of photosynthesis. The amino-terminai sequences of the L, M, and H subunits and the nucleotide and derived amino acid sequences of the L and M structural genes from Rhodopseudomonas sphaeroides have previously been determined. We report here the sequence of the H subunit, completing the primary structure determination of the reaction center from R. sphaeroides. The nucleotide sequence of the gene encoding the H subunit was determined by the dideoxy method after subcloning fragments into single-stranded M13 phage vectors. This information was used to derive the amino acid sequence of the corresponding polypeptide. The termini of the primary structure of the H subunit were established by means of the amino and carboxy terminal sequences of the polypeptide. The data showed that hte H subunit is composed of 260 residues, corresponding to a molecular weight of 28,003. A molecular weight of 100,858 for the reaction center was calculated from the primary structures of the subunits and the cofactors. Examination of the genes encoding the reaction center shows that the codon usage is strongly bviased towards codons ending in G and C. Hydropathy analysis of the H subunit sequence reveals one stretch opf hydrophobic residues near the amino terminus; the L and M subunits contain five such stretches. From a comparison of the sequences of homologous proteins found in bacterial reaction centers and photosystem II of plants, an evolutionary tree was contructed. The analysis of evolutionary relationships showed that the L and M subunits of reaction centers and D1 and D2 proteins of photosystem II are descended from a common ancestor, and that the rate of change in these proteins was much higher in the first billion years after the divergence of the reaction center and photosystem II than in the subsequent billion years represented by the divergence of the species containing these proteins.
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    URL: http://dx.doi.org/10.1002/prot.340010405
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    Sequence conservation and region shuffling in an endoglucanase and an exoglucanase from Cellulomonas fimi (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 335-341 
    Details
    ISSN: 0887-3585
    Keywords: cellulases ; active sites ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Cellulomonas fimi produces an endoglucanase and an exoglucanase which bind strongly to cellulose. Each enzyme contains three distinct regions: a short sequence of about 20 amino acids containing only proline and threonine (the ProThr box); an irregular region, rich in hydroxyamino acids, of low charge density, and which is predicted to have little secondary structure; and an ordered region of higher charge density which contains a potential active site, and which is predicted to have secondary structure; and an ordered region of higher charge density which contains a potential active site, and which is predicted to have secondary structure. The Pro-Thr box is conserved almost perfectly in the two enzymes. The irregular regions are 50% conserved, and the conserved sequences include four Asn-Xaa-Ser/Thr sites. The ordered regions appear not to be conserved, but the potential active sites both have the sequence Glu-Xaa7-Asn-Xaa6-Thr; they occur at widely separated sites in the two regions. The order of the regions is reversed in the two enzymes: irregular-Pro-Thr box-ordered in the endoglucanase; ordered-Pro-Thr box irregular in the exoglucanase. The genes for the two enzymes appear to have arisen by shuffling of two conserved sequences and either one or two other sequences.
    Additional Material: 6 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010407
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    Proteases of enhanced stability: Characteization of a thermostable variant of subtilisin (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 326-334 
    Details
    ISSN: 0887-3585
    Keywords: thermal stability ; protein engineering ; mutagenesis ; plate assay ; thermophilic enzymes ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A Procedure has been developed for the isolation and identification of mutants in the bacterial serine protease subtilisin that exhibit enhanced thermal stability. The cloned subtilisin BPN'gene from Bacillus amyloliquefaciens was treated with bisulfite, a chemical mutagen that deaminates cytosine to uracil in single-stranded DNA. Strains containing the cloned, mutagenized subtilisin gene which produced subtilisin with enhanced thermal stability were selected by a simple plate assay procedure which screens for esterase activity on nitrocellulose filters after preincubation at elevated temperatures. One thermostable subtilisin variant, designated 7150, has been fully characterized and found to differ from wild-type subtilisin by a single substitution of Ser for Asn at position 218. The 7150 enzyme was found to undergo thermal inactivation at onefourth the rate of the wild-type enzyme when incubated at elevated temperatures. Moreover, the midpoint in the thermally induced transition from the folded to unfolded state was found to be 2.4-3.9°C higher for 7150 as determined by differential scanning calorimetry under a variety of conditions. The refined, 1.8-Å crystal structures of the wild-type and 7150 subtilisin have been compared in detail, leading to the conclusion that slight improvements in hydrogen bond parameters in the vicinity of position 218 result in the enhanced thermal stability of 7150.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010406
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    Predicting antibody hypervariable loop conformations II: Minimization and molecular dynamics studies of MCPC603 from many randomly generated loop conformations (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 342-362 
    Details
    ISSN: 0887-3585
    Keywords: antibodies ; immunoglobulins ; conformation prediction ; energy minimazation ; random stranting conformations ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: We describe a method for predicting the conformations of loops in proteins and its application to four of the complementarity determining regions [CDRs] in the crystallographically determined structure of MCPC603. The method is based on the generation of a large number of randomly generated conformations for the backbone of the loop being studied, followed by either minimization or molecular dynamics followed by minimization starting from these random structures. The details of the algorithm for the generation of the loops are presented in the first paper in this series (Shenkin etal.[submitted]). The results of minimization and molecular dynamics applied to these loops is presented here. For the two shortest CDRs studied (H1 and L2, which are five and seven amino acids long), minimizations and dynamics simulations which ignore interactions of the loop amino acids beyond the carbon ture closely. This suggests that these loops fold independently of sequence variation. For the third CDR (L3, which is nine amino acids), those portions of the CDR near its base which are hydrogen bonded to framework are well replicated by our procedures, but the top of the loop shows singificant conformational variability. This variability persists when side chain interactions for the MCPC603 sequence are included. For a fourth CDR (H3, which is 11 amino acids long), new low-energy backbone conformations are found; however, only those which are close to the crystal are compatible with the sequence when side chain interactions are taken into account. Results from minimuzation and dynamics on single CDRs with all other CDRs removed are presented. These allow us to explore the extent to which individual CDR conformations are determined by interactions with framework only.
    Additional Material: 6 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010408
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    Multiple conformations of amino acid residues in ribonuclease A (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 370-375 
    Details
    ISSN: 0887-3585
    Keywords: enzyme structure ; disorder ; refinement ; high resolution ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The highly refined 1.26 Å structure (R = 0.15) of phosphate-free bovine pancreatic ribonuclease A was modeled with 13 residues having discrete multiple conformations of side chains. These residues are widely distributed over the protein surface, but only one of them, Lys 61, is involved in crystal packing interactions. The discrete conformers have no unusual torsion angles, and their interactions with the solvent and with other atoms of the protein are similar to those residues modeled with a single conformation. For three of the residues-Val 43, Asp 83, and Arg 85-two correlated conformations are found. The observed multiple conformations on the protein surfaces will be of significance in analyzing structure-function relationships and in performing protein engineering.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010410
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    Structural features of ribonucleotide reductase (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 376-384 
    Details
    ISSN: 0887-3585
    Keywords: ribonucleotide reductase ; unique N-terminal domain ; nucleotide binding site ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Herpes simplex virus type 1 (HSV-1) encodes a ribonucleotide reductase which comprises two polypeptides with sizes of 136,000 (RR1) and 38,000 mol. wt. (RR2). We have determined the entire DNA sequence specifying HSV-1 RR1 and have identified two adjacent open reading frames in varicella-zoster virus (VZV) which have homology to HSV RR1 and RR2; the predicted sizes for the VZV RR1 and RR2 polypeptides are 87,000 and 35,000 mol. wt. respectively. Amino acid comparisons with RR1 and RR2 polypeptides from other organisms indicate that HSV-1 RR1 contains a unique N-terminal domain which is absent from other RR1 polypeptides apart from HSV-2 RR1. These N-terminal amino acid sequences are poorly conserved between HSV-1 and HSV-2 in contrast to the remainder of the protein which shows greater than 90% homology. Polypeptide structural predictions suggest that the HSV-1 N-terminal domain may be separated into two regions, namely, a β-sheet structure followed by a nonstructured area. Across the remainder of RR1 and RR2, comparisons also reveal blocks of amino acids conserved between the different ribonucleotide reductases, and these may be important for enzyme activity. From predictions on the structure of these conserved blocks, we have proposed that the location of a substrate binding site within RR1 is centered on three conserved glycine residues in a region which is predicted to adopt a β-sheet/turn/α-helical structure;this approximates to the structure for ADP nucleotide binding folds. Finally, we propose that the promoters for the HSV and Eptein-Barr virus (EBV) RR2 transcripts have evolved by separate evolutionary routes.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010411
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    Primary structure of a precursor to the asprartic proteinase from Rhizomucor miehei shows that the enzyme is synthesized as a zymogen (1986)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 1 (1986), S. 363-369 
    Details
    ISSN: 0887-3585
    Keywords: cDNA library ; disulphide bridges ; prosegment homology ; mRNA structure ; N-glycosylation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In order to characterize the zymogen of the milk-clotting enzyme from Rhizomucor miehei, we constructed a cDNA library on pBR327 in Escherichia coli. Aspartic proteinase-specific recombinants were isolated by colony hybridization to a specific oligonucleotide mixture, and the cDNA sequence corresponding to a precursor form of the enzyme was determined.The decuced amino sequence shows that this secreted fungal proteinase is synthesized as a precursor. The first 22 amino acid residues in this precursor constitute a typical signal peptide. The amino acid sequence of the following 47-amino-acid-long prosegment shows homology to the prosegments from both the extracellular and intracellular vertebrate aspartic proteinases, and to the prosegments from the yeast and Mucor pusillus aspartic proteinases as well. These observations suggest that all aspartic proteinases are synthesized with a prosegment and that this prosegment is essential for the correct folding of all the mature enzymes. The active Rhizomucor miehei enzyme consists of 361 amino acide residues with a total molecular weight of 38,701. Clusters of idendtities around the active site cleft support the assumption that these proteinasess have a common folding of their peptide chains. The disulphide bridges were localized in the fungal enzyme, and 2 N-glycosylation sites were identified.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/prot.340010409
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    Intracellular particle motions (cytoplasmic streaming) in staminal hairs of Setcreasea purpurea: Effect of azide and low temperature (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 305-313 
    Details
    ISSN: 0886-1544
    Keywords: cytoplasmic streaming ; Setcreasea purpurea ; intracellular particle movements ; intercellular transport ; azide ; low temperature ; calcium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cytoplasmic streaming and its response to azide and low temperature were examined by using high-resolution video-enhanced light microscopy in Setcreasea purpurea staminal hair cells of immature flowers. Particles and organelles examined moved along well-defined pathways, in repeated and unequal saltatory steps, at different rates and sometimes against the main direction of flow (bidirectionally) in both transvacuolar strand and peripheral cytoplasm. Particle movements were reversibly inhibited with azide. Low temperatures caused transvacuolar strands to shift or break. This cytoplasm accumulated in areas outside of the vacuole where spherosomes continued to saltate, but not along well-defined pathways. In the peripheral cytoplasm, however, the spherosomes continued to move normally, amyloplasts became swollen, and they plus the other organelles (except spherosomes) were stationary. Normal particle movements were obtained when chilled cells were rewarmed to 27°C for ca 15 min.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060307
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    Masthead (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060101
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    Sperm chemotaxis in siphonophores: Identification and biochemical properties of the attractant (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 225-228 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060222
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    Computer simulation of bend propagation by axoplasmic microtubules (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 347-353 
    Details
    ISSN: 0886-1544
    Keywords: axoplasmic transport ; flagella ; microtubule ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The generation of bending waves by microtubules in squid nerve axoplasm has been modelled using appropriately modified versions of computer programs developed previously for simulation of flagellar bending waves. The results confirm that a constant longitudinal force directed along the axis of the microtubule is sufficient to cause the generation of regular oscillations and propagated bending waves when the forward gliding movement of the microtubule is obstructed. No control mechanism is required to modulate the active force-generating system. In order to obtain bending waves similar to those observed experimentally, it was necessary to use a model for the force-generating system in which the active force decreases with increasing sliding velocity. If the elastic bending resistance of axoplasmic microtubules is similar to that of microtubules in sperm terminal filaments, the longitudinal force per unit length generated by the axoplasmic microtubules must be of the same order of magnitude as the force generated by dynein arms along the doublet microtubules of eukaryotic flagella.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060311
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    Influence of translocation track on the motion of intra-axonally transported organelles in human nerve (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 339-346 
    Details
    ISSN: 0886-1544
    Keywords: axonal transport ; human nerve ; video-enhancement ; digital image processing ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The mechanism by which organelles are transported bidirectionally in axoplasm is still unknown; however, evidence of a key role for microtubules in many nonmammalian models has been established. We have observed common or shared tracks within the axoplasm of human nerves along which multiple organelles of varying size and shape are bidirectionally transported. Organelles traveling anterogradely and retrogradely were visualized by video-enhanced differential interference contrast optics and analyzed with the aid of computer-image-processing techniques.Speeds of translocating organelles were determined at eight to 16 translocation points along a path or “track.” Each translocation speed was plotted against its corresponding position on the track to develop a “speed/position diagram.” Regardless of mean organelle speed or direction of motion, organelles sharing a common track exhibited similar patterns of “speeding up” and “slowing down” relative to position along the track. Speed position data for organelles translocating the local axonal region of a common track showed no unique patterns (not different from a uniform distribution, p 〈 0.05). The unique speed/position patterns exhibited by common tracks were not necessarily related to the patterns of other tracks in the immediate vicinity (distance between tracks of 〈 0.50 μm). These findings suggest that (1) there are “common tracks” shared by organelles moving retrogradely and anterogradely; (2) both the organelles and the “track” associated with its translocation play a role in the resultant motion of that organelle; (3) the influence exerted by a common track on the motion of an organelle results in a pattern of speed changes related to position along the track.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060310
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    Naturally occurring tubulin-containing paracrystals in Allogromia: Immunocytochemical identification and functional significance (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 363-375 
    Details
    ISSN: 0886-1544
    Keywords: Allogromia ; cytoplasmic transport ; microtubules ; reticulopod withdrawal ; tubulin-containing paracrystal ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Bundles of microtubules (MTs) are readily visualized in vivo by videomicroscopy in highly flattened reticulopodia of the foraminiferan protozoan Allogromia sp. strain NF. In this report we use videomicroscopy, immunocytochemistry, and high-voltage electron microscopy to characterize the dynamic changes that occur in this extensive MT cytoskeleton, and in the associated cytoplasmic transport, during induced withdrawal and subsequent reextension of reticulopodia. Within seconds after application of the withdrawal stimulus (seawater substitute made hypertonic with MgCl2) intracellular bidirectional transport along linear MT-containing fibrils ceases and is replaced by an inward, constant-velocity flow of cytoplasm along the fibrils. As withdrawal continues, most fibrils become wavy and coalesce to form phase-dense pools. These wavy fibrils and phase-dense pools contain a paracrystalline material and few if any MTs. Same-section correlative immunofluorescence and high-voltage electron microscopy reveal that the paracrystalline material contains tubulin. During recovery linear fibrils (MTs) rapidly extend from the phase-dense pools (paracrystals), which concurrently shrink in size, thus reestablishing normal network morphology and motility. We conclude that the MT cytoskeleton in Allogromia reticulopodia is transfonned during withdrawal into a tubulin-containing paracrystal, which serves as a temporary reservoir of MT protein and an initiation site for MT regrowth.
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    URL: http://dx.doi.org/10.1002/cm.970060403
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    Independence of centriole formation and initiation of DNA synthesis in Chinese hamster ovary cells (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 355-362 
    Details
    ISSN: 0886-1544
    Keywords: centriole ; DNA synthesis ; cell cycle ; Chinese hamster ovary cells ; taxol ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The relationship between centriole formation and DNA synthesis was investigated by examining the effect of taxol on the centriole cycle and the initiation of DNA synthesis in synchronized cells. The centriole cycle was monitored by electron microscopy of whole-mount preparations [Kuriyama and Borisy, J. Cell Biol., 1981, 91:814-821]. A short daughter centriole appeared in perpendicular orientation to each parent during late G1 or early S and elongated slowly during S to G2. Addition of 5-20 μg/ml taxol to a synchronous population of cells in S phase did not inhibit centriole elongation; rather, elongation was accelerated. In contrast, when taxol was added to M phase or early G1 cells, centriole duplication was completely inhibited. The taxol block was reversible since nucleation and elongation of centrioles resumed as soon as the drug was removed. Cells exposed to taxol progressed through the cell cycle and became blocked in mitosis, as indicated by an increase in the mitotic index, but eventually the mitotic arrest was overcome, resulting in formation of multinucleated cells. A peak in mitotic index was seen in the following generation, indicating that chromosomes duplicated in the presence of taxol. Incorporation of 3H-thymidine followed by autoradiography confirmed that DNA synthesis was initiated in the presence of taxol even though formation of daughter centrioles was inhibited. It seems, therefore, that centriole duplication is not a prerequisite for entry into S phase. Since DNA synthesis has already been demonstrated not to be necessary for centriole duplication, these two events, normally coordinated in time, appear to be independent of each other.
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    URL: http://dx.doi.org/10.1002/cm.970060402
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    Evidence for an interaction between the cell surface and intermediate filaments in cultured fibroblasts (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 389-405 
    Details
    ISSN: 0886-1544
    Keywords: cell membrane complex ; extracellular matrix ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Intermediate filaments (IF) were found in close proximity to the plasma membrane in substrate attached baby hamster kidney cells (BHK-21) and chick embryo fibroblasts (CEF) as well as cells removed from their substrate in the absence of trypsin. However, in cells removed with trypsin, it appeared that IF had retracted away from the membrane. In cells with abundant extracellular matrix (ECM), colchicine induced massive cables of IF, which appeared to interact with specialized areas of the inner plasma membrane. In cells lysed to extract most microfilaments and cytoplasmic constituents, the intact IF network which remained was closely associated with the ECM. From these ultrastructural observations it was concluded that IF interact in some way with a “cell membrane complex” defined as comprising the plasma membrane and molecules attached to its inner and outer surfaces.In order to investigate the possibility that components of the membrane complex may co-isolate with IF, native intermediate filaments (NIF) were prepared. In addition to the structural subunits and other associated polypeptides, a ∼220 kd species which reacted specifically with antibodies directed against the ECM protein fibronectin (FN) was observed; 220 kd was still present after NIF were isolated under pH conditions where FN is more soluble, suggesting that its presence was not simply due to the coprecipitation of two insoluble proteins. Immunofluorescence and immunogold localization confirmed that FN is a component of the cell membrane complex with which IF appeared to interact.
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    URL: http://dx.doi.org/10.1002/cm.970060405
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    Structure and composition of the cytoskeleton of nucleated erythrocytes: III. Organization of the cytoskeleton of Bufo marinus erythrocytes as revealed by freeze-dried platinum-carbon replicas and immunofluorescence microscopy (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 376-388 
    Details
    ISSN: 0886-1544
    Keywords: marginal band ; spectrin ; vimentin ; surface-associated cytoskeleton ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Platinum-carbon (Pt-C) replicas of freeze-dried erythrocyte cytoskeletons of the toad, Bufo marinus, were prepared using a modified Balzers 300 system. Examination in stereo of replicas of the microtubule-containing marginal band revealed filaments projecting from the microtubule walls to form links between adjacent microtubules. These cross-bridging proteins may bundle the microtubules into the configuration of the marginal band (MB) and may also serve to stabilize the structure. The MB appears to have linkages to components of the surface-associated cytoskeleton (SAC). The SAC forms a continuous matrix that spreads across the upper and lower surfaces of the cell adjacent to the plasma membrane and extends around the outer perimeter of the MB. Thus, the SAC encapsulates the MB and the central nucleus. After lysis, the elements of the cytoskeleton remain in a configuration similar to that found in the whole cell. Spectrin (fodrin) and actin were identified by immunofluorescence in the region of the SAC. When labeled with antibodies specific for vimentin and synemin, a network of intermediate filaments can be detected in the region between the nucleus and the MB. These vimentin filaments are also enclosed within the SAC and appear in Pt-C replicas to emerge from the area of the nuclear envelope. As the filaments extend toward the periphery of the cell, they form attachments to the SAC. Attachments of intermediate filaments to both the nucleus and the SAC thus appear to anchor the nucleus in its central position within the cytoskeleton.
    Additional Material: 11 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060404
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    Masthead (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060501
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    Malorientation and abnormal segregation of chromosomes during recovery from Colcemid and Nocodazole (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 419-427 
    Details
    ISSN: 0886-1544
    Keywords: colcemid ; nocodazole ; kinetochores ; microtubules ; spermatocytes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Reversal of meiotic arrest in crane-fly spermatocytes by U.V. irradiation of Colcemid-arrested cells or by rinsing Nocodazole-arrested cells in fresh buffer results in the induction of chromosome malorientation. Malorientations observed among Colcemid-recovering and Nocodazole-recovering spermatocytes at frequencies higher than normally observed in untreated cells included associations of sister kinetochores of half-bivalents with both spindle poles (amphitely), in contrast with associations of sisters with only one pole (syntely) as is usually found during the first meiotic division. In several cases, prior to anaphase onset, maloriented bivalents appeared unusually tilted with respect to the spindle axis, and during anaphase they gave rise to laggard half-bivalents that did not segregate during anaphase along with half-bivalents having proper syntelic orientation. The results parallel previous findings obtained during cold recovery, and the properties of the drugs used here suggest that their action on microtubules, although reversible, induces malorientation during recovery from meiotic arrest.
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    URL: http://dx.doi.org/10.1002/cm.970060407
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    Kinetochore microtubules in crane-fly spermatocytes: Untreated, 2°C-treated and 6°C-grown spindles (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 428-438 
    Details
    ISSN: 0886-1544
    Keywords: kinetochores ; spindle apparatus ; anaphase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We investigated the involvement of kinetochore microtubules (kMTs) in mediating chromosome-to-pole connections in crane-fly (Nephrotoma suturalis and Nephrotoma ferruginea) spermatocytes. Two experimental treatments were used to yield spindles with reduced numbers of nonkinetochore microtubules (nkMTs). Short-term (10-15 min) exposure of spermatocytes to 2°C caused depolymerization of the majority of nkMTs, resulting in a kMT:(kMT + nkMT) ratio of 0.76. Long-term (24h) exposure to 2°C followed by recovery at 6°C resulted in a kMT:(kMT + nkMT) ratio of 0.55, the spindle having more nkMTs than a 2°C-treated spindle but fewer than an untreated spindle, in which the kMT:(kMT + nkMT) ratio was 0.27. The numbers and lengths of kMTs in 6°C-grown spindles were similar to those in untreated cells, suggesting that the overall inhibition of MT assembly at 6°C apparently did not affect the mechanism by which kMTs are formed. We observed most kMTs of early anaphase spindles to be long (〉3 μm), and many extended to the polar regions of the spindle. Thus, the crane-fly spindle appears not to be as atypical as it was previously suggested to be.
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    URL: http://dx.doi.org/10.1002/cm.970060408
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    Relationship between intermediate filaments and microfilaments in cultured fibroblasts: Evidence for common foci during cell spreading (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 406-418 
    Details
    ISSN: 0886-1544
    Keywords: Intermediate filaments ; microfilaments fibroblast cell spreading ; focal center ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Spreading and fully spread chick embryo fibroblasts (CEF) were examined by double-label fluorescence microscopy using the actin-specific probe rhodamine-phalloidin and an antibody directed against CEF intermediate filaments (IF). During midspreading, a striking relationship became discernible: statistical analysis showed that approximately half of the cell population exhibited one or more phase-dense, phalloidin-binding nodules that appeared to act as foci from which IF diverged. Coincidence between actin-containing structures and IF was not limited to these centers; IF could also frequently be seen running in close parallel arrays with stress fibers.Ultrastructural analysis confirmed the presence of non-membrane-bound out-pocketings along the length of stress fibers from which 10-nm IF diverged. These structures varied in size and shape, and displayed a dense, fine fibrillar appearance. IF and microfilaments (MF) were distinguished by size and by decoration of MF with myosin subfragment-1. Other IF-MF interactions were seen in cells of all stages: IF were observed to loop through stress fibers, most frequently at the cell margins. In colchicine-treated cells, IF became redistributed into cables that often ran parallel and appeared to merge with stress fibers. Cytochalasin D-treated CEF exhibited loose aggregates of actin-containing material that appeared to be associated with IF.These results suggest the possibility of an interaction between actin-containing structures and IF, particularly during cell spreading in cultured fibroblasts.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060406
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  • 79
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    Dynamic aspects of the contractile system in Physarum Plasmodium: I. Changes in spatial organization of the cytoplasmic fibrils according to the contraction-relaxation cycle (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 439-447 
    Details
    ISSN: 0886-1544
    Keywords: dynamics of actomyosin fibril ; microfilament bundle ; NBD-phallacidin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Dynamic changes in the spatial organizations of cytoplasmic fibrils (microfilament bundles) related to the contraction-relaxation cycle in thin-spread plasmodia of Physarum polycephalum were investigated by fluorescence microscopy, where NBD-phallacidin was used to stain the fibrils, combined with polarizing light microscopy.The fibrillar organization in the anterior region, which consists of a fanlike spreading plasmodial sheet, strikingly changed according to the phase of the cycle. In the early stage of the contraction, as the endoplasm began to stream backward, the fibrils developed into a number of slender and flabby fibrils emanating from the inside of the cell membrane and the nodes. They became thicker and more straightforward fibrils running parallel to each other at the middle stage, and finally formed a thick framework consisting of a “polygonal network” near the tip of the migrating front and a “parallel array” in the inner part. In the relaxation phase, as the endoplasm streamed forward, the fibrillar framework disintegrated gradually and finally disappeared almost completely, remaining only around the nodes in some cases.The fibrillar patterns in the posterior region, which consists of ramified strands, showed no conspicuous rhythmic change with alternation of the streaming direction.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060502
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  • 80
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    Dynamic aspects of the contractile system in Physarum Plasmodium: II. Contractility of triton cell models in accordance with the contraction and relaxation phases of the plasmodia (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 448-457 
    Details
    ISSN: 0886-1544
    Keywords: cytoplasmic fibril ; birefringence ; microfilament ; contraction-relaxation cycle ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The contractility of Physarum plasmodium was investigated using cell models that were prepared by treating thin-spread plasmodia with ice-cold 0.2% Triton X-100. Cell models obtained from the anterior regions of the thin-spread plasmodia in the contraction phase retained many birefringent cytoplasmic fibrils. The fibrils vigorously contracted on addition of ATP, inducing simultaneous contraction of the whole cell models. In contrast, cell models prepared from the anterior regions in the relaxation phase scarcely contained the birefringent fibrils and exhibited only weak contractility on addition of ATP. The posterior regions of the thinspread plasmodia, which were composed of ramified plasmodial strands, always retained many fibrils when treated with the Triton solution and showed intensive contraction on addition of ATP.SDS-polyacrylamide gel electrophoresis showed that the model was enriched for actin and myosin. About 40% of the actin was extracted from the plasmodium by the Triton treatment, while scarcely any myosin was extracted.Fragmin, a F-actin-fragmenting factor, caused the birefringent fibrils to diminish in the presence of Ca2+, but more than 30 minutes was required for their complete disappearance. The birefringent fibrils weakened by 30-minute fragmin treatment disappeared immediately on addition of ATP or AMP-PNP.
    Additional Material: 9 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060503
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  • 81
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    Effects of taxol on microtubule arrays in cultured higher plant cells (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 469-478 
    Details
    ISSN: 0886-1544
    Keywords: plant microtubules ; mitosis ; cytokinesis ; plant cell culture ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Treatment with 10 μm taxol disrupted mitotic and cytoplasmic arrays of microtubules (MT) in cultured cells of two higher plants, Vicia hajastana (vetch) and Zinnia elegans. When treated for 1, 24, and 48 h, cells in both cultures showed similar effects. After 1 h, multipolar arrays of MT were noted in prophase, large aster-like arrays of MT appeared in metaphase, and extra MT shared poles with otherwise normal-appearing metaphase and anaphase configurations. After 24 and 48 h, some phragmoplasts were multipartite or misplaced. In interphase cells, micronuclei and multinucleate cells were evidence of irregular mitosis and cytokinesis. Cytoplasmic MT in elongated cells were oriented parallel to, instead of at right angles to the long axis of the cell. Some interphase cells lost asymmetry while maintaining organized arrays of MT. Taxol appears to disrupt mitotic and cytoplasmic arrays of MT, seemingly overriding the mechanism(s) regulating MT polymerization and orientation.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060505
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  • 82
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    Cytoskeletal architecture of reactivated crayfish axons, with special reference to crossbridges among microtubules and between microtubules and membrane organelles (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 458-468 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; axoplasm ; fast flow ; quick-freeze ; deep-etch ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Bidirectional organelle movements were observed in fresh and permeabilizedreactivated (0.02% saponin, 5 mM Mg++ ATP) walking leg axons of crayfish with video-enhanced contrast, differential interference contrast (AVEC-DIC) microscopy; and the cytoskeletal organization of those axons was studied with quickfreeze, deep-etch electron microscopy (QF,DE) to understand the structure of the microtubule (MT) domain and to determine the basic cytoskeletal structures necessary for organelle transport in vivo. Vesicles and mitochondria moved bidirectionally in the central parts of fresh or permeabilized-reactivated axons. Although the axoplasm of the fresh axon was composed of longitudinally oriented microtubules and granular materials in which membrane organelles were embedded, a network of fine strands existed in the core of the granular materials. Crossbridges between membrane organelles and microtubules were present. In the central part of reactivated axons, the cytoskeleton consisted of microtubules, highly anastomosing networks of fine strands (6.6 ± 1.4 nm in width) that crosslinked the microtubules with each other, and relatively short, straight crossbridges (25 ± 3.9 nm in length, 5.5 ± 2.1 nm in width) crosslinking membrane organelles with microtubules. It has been shown that a 270KD microtubule associated protein (MAP) could be a main component of crossbridges between MTs [Hirokawa, 1986]. Hence the dynamic conformational change of crossbridges between membrane organelles and microtubules could play an important role when membrane organelles are transported.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060504
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  • 83
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    Effects of pteridines on the filopodia of Dictyotelium discoideum vegetative amoebae (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 479-484 
    Details
    ISSN: 0886-1544
    Keywords: motility ; chemotaxis ; chemoattractant ; cytoskeleton ; folic acid ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Living vegetative amoebae of NC-4H Dictyostelium discoideum were studied to determine if a variety of pteridines had any effect on the filopodia. We observed that production, elongation, and branching of these filopodia were stimulated by pteridines that are chemoattractants for cells of this strain. This stimulation occurs at chemotactically effective concentrations and is observed before motility is evident. A relationship between filopodia and chemoattractant signal processing is discussed.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060506
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  • 84
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    Video analysis of chemotactic locomotion of stored human polymorphonuclear leukocytes (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 485-491 
    Details
    ISSN: 0886-1544
    Keywords: PMN chemotaxis ; PMN storage ; PMN locomotion ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Previous studies of the storage of polymorphonuclear leukocytes (PMNs) have used an empirical approach to define “optimal” conditions. To date, no storage conditions have been described which satisfactorily preserve the chemotactic function of PMNs beyond 24 h. In an effort to define the precise nature of the storage lesion, we studied the chemotactic locomotion of freshly isolated PMNs and PMNs which had been suspended in citrate-phosphate-dextrose-adenine (CPD-Al) plasma and stored in PVC bags, at 20-22°C for 24 h. We used time-lapse video recording and computer image analysis to quantitate the motion of PMNs migrating under agarose. The positions of individual motile cells were traced at 1-min intervals for 5 min. The following parameters were used to quantitate migration: (1) speed (distance/min), (2)) persistence of locomotion index (velocity/speed), (3) orientation angle (the angle of the vector describing the next displacement of a cell relative lo a direct line toward the chemoattractant), and (4) chemotropic index (cosine of the orientation angle). After 24 h of storage, the following changes were observed: (1) fewer cells migrated, (2) (he speed of migrating cells was reduced by 25%, (3) the persistence of locomotion index decreased by 7%, which indicates that migrating cells made slightly more/wider turns, and (4) the chemotropic index was decreased by 30%, which indicates that migrating cells were less accurate in their orientation toward the chemoattractant. Apparently, the storage of PMNs selectively impairs the ability of some cells to orient accurately in a chemotactic gradient and changes the distribution of these locomotor parameters within the population.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060507
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  • 85
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    Bivalent orientation and behavior in crane-fly spermatocytes recovering from cold exposure (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 492-501 
    Details
    ISSN: 0886-1544
    Keywords: chromosome orientation ; prometaphase ; meiosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: At metaphase in crane-fly primary spermatocytes, the two sister kinetochores at the centromere of each homologue in a bivalent normally are adjacent and face the same pole; one homologue has all its kinetochore microtubules (kMTs) extending toward one pole and its partner has all its kMTs extending toward the opposite pole. In contrast, during recovery from exposure to 2°C, one or both homologues in many metaphase bivalents had bipolar malorientations: all kMTs of one kinetochore extended toward one pole and some or all those of its sister extended toward the other. Metaphase sister kinetochores that had most of their kMTs extending toward the same pole were adjacent, and those with most extending toward opposite poles were separated from each other. Distances between homologous centromeres were similar to those in properly oriented bivalents. Maloriented bivalents were tilted relative to the spindle axis, and analysis of living cells showed that tilted configurations were rare during prometaphase in untreated cells but frequently arose in cold-recovering cells as initial configurations, then persisted through metaphase. This was in contrast to unipolar configurations of bivalents (configurations suggesting orientation of both homologous centromeres toward the same pole), which always reoriented shortly after the configuration arose. We conclude that in cold-recovering cells, bipolar malorientations are more stable than unipolar malorientations, and the orientation process is affected such that bipolar malorientations arise in bivalents upon initial interaction with the spindle and persist through metaphase.
    Additional Material: 6 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060508
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  • 86
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    Rhamnolipid from Pseudomonas aeruginosa inactivates mammalian tracheal ciliary axonemes (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 502-509 
    Details
    ISSN: 0886-1544
    Keywords: respiratory cilia ; dynein ; ATPase ; cystic fibrosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Isolated ciliary axonemes from pig trachea were exposed to increasing concentrations of purified Pseudomonas aeruginosa rhamnolipid. This is a defined ciliary system allowing observation of direct impairment of functional axonemes. Axonemal motility and ATPase activity were decreased in proportion to rhamnolipid concentrations. ATPase-associated proteins observed in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and dynein arms seen in ultrastructural cross sections progressively disappeared from axonemes with exposure to rhamnolipid. These four independent measures establish that the rhamnolipid removes the ATPase-containing outer dynein arms from the ciliary axoneme, thereby rendering the axoneme immotile.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060509
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  • 87
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    Announcing a 1987 UCLA symposium (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. i 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060512
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  • 88
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    Masthead (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986) 
    Details
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060601
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  • 89
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    Cytoskeletal architecture and motility in a giant freshwater amoeba, Reticulomyxa (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 521-533 
    Details
    ISSN: 0886-1544
    Keywords: intracellular organelle transport ; microtubules ; microfilaments ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Reticulomyxa is a large, multinucleated freshwater protozoan with striking intracellular transport. Cyloplasmic streaming and saltatory movements of individual organelles (at rates of up to 25 μm/sec) are observed within the naked cell body and the extensive reticulate peripheral network of fine cytoplasmic strands. As demonstrated by video-enhanced light microscopy, individual organelles move only when associated with cytoskeletal linear elements. The linear elements are composed of mixed colinear bundles of microtubules and actin filaments, which form the backbone of the reticulopodial network. The constant branching, sprouting, and fusion of network stands suggest unique membrane properties and an unusually dynamic cytoskeleton. The electrophoretic mobility of Reticulomyxa tubulins and the lack of crossreactivity with several antibodies known to react with many plant and animal tubulins suggest that they may differ from other tubulins more widely than might be expected. Reticulomyxa's large size, the rapidity and pervasiveness of the two forms of transport, and the simple and ordered cytoskeleton make the organism well suited for future studies on the mechanisms of intracellular transport.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060511
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  • 90
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    Polarized microtubule gliding and particle saltations produced by soluble factors from sea urchin eggs and embryos (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 537-548 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; sea urchins ; kinesin ; mitosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In this report, we describe an in vitro system for analyzing microtubule-based movements in supernatants of sea urchin egg and embryo homogenates. Using video enhanced DIC microscopy, we have observed bidirectional saltatory particle movements on native taxol-stabilized microtubules assembled in low speed supernatants of Lytechinus egg homogenates, and gliding of these microtubules across a glass surface. A high speed supernatant of soluble proteins, depleted of organelles, microtubules, and their associated proteins supports the gliding of exogenous microtubules and translocation of polystyrene beads along these microtubules. The direction of microtubule gliding has been determined directly by observation of the gliding of flagellar axonemes in which the (+) and (-) ends could be distinguished by biased polar growth of microtubules off the ends. Microtubule gliding is toward the (-) end of the microtubule, is ATP sensitive, and inhibited only by high concentrations of vanadate. These characteristics suggest that the transport complex responsible for microtubule gliding in S2 is kinesin-like. The implications of these molecular interactions for mitosis and other motile events are discussed.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060602
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  • 91
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    Decoration of microtubules by fluorescently labeled microtubule-associated protein 2 (MAP2) does not interfere with their spatial organization and progress through mitosis in living fibroblasts (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 570-579 
    Details
    ISSN: 0886-1544
    Keywords: microinjection ; mitosis ; microtubule-associated proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Microtubule-associated protein 2 (MAP2) derivatized with iodoacetamidotetramethylrhodamine or with iodoacetamidofluorescein binds to microtubules after injection into living interphase cells [Scherson et al, 1984]. The binding of derivatized MAP2 stabilized microtubules in vitro; it was therefore important to check if the binding of MAP2 in vivo perturbed the dynamics and organization of the microtubule network. We have addressed these questions by studying the effect of the injection of derivatized MAP2 on mitosis in PtK 1 cells and on the recovery of the microtubule network from low temperature incubation in interphase cells. We found that the presence of derivatized MAP2 did not change the duration of any mitotic stage and that the injected cell normally completed mitosis. We subsequently showed that the injected MAP2 bound to the microtubules within 5 minutes after injection and remained bound throughout the course of mitosis. The reorganization of the microtubule network upon cooling and rewarming was studied in the cytoplasm of human foreskin fibroblasts (356 cells). During the recovery, the distribution of the fluorescent MAP2 in living cells was identical with the microtubule pattern visualized by immunofluorescence in lysed and fixed cells.In these experiments, the fluorescent MAP2 bound to microtubules can be considered as a nonperturbing reporter of the microtubule network. This result is discussed in terms of the role of MAPs in the dynamics and organization of microtubules in living cells.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060605
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  • 92
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    Cyclical bending of two outer-doublet microtubules in frayed axonemes of Chlamydomonas (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 580-585 
    Details
    ISSN: 0886-1544
    Keywords: flagella ; microtubules ; Chlamydomonas ; bending movement ; oscillation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: When detergent-extracted cell models of Chlamydomonas reinhardtii were left in the presence of 1 mM Mg-ATP for more than 30 minutes flagellar axonemes tended to become frayed into fine bundles of microtubules. Under such conditions, bundles made up of a pair of outer-doublet microtubules displayed oscillatory bending movements of low (〈 2 Hz) frequencies. The two doublet microtubules underwent association-dissociation cycles coupled with gross bending movement. A model is presented to explain this phenomenon by unidirectional sliding interaction between the two microtubules.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060606
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  • 93
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    Theoretical analysis of radioactivity profiles during fast axonal transport: Effects of deposition and turnover (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 620-627 
    Details
    ISSN: 0886-1544
    Keywords: radiolabeled organelle profile ; retrograde transport system ; anterograde transport system ; turnover ; nodes of Ranvier ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In a preceding study [Blum, J.J., and Reed, M.C. (1985): Cell Motil. 5:507-527], factors responsible for the shape and velocity of the leading edge of the radiolabeled organelle profile were analyzed, but processes that might influence the shape of the plateau-like region behind the advancing wave were ignored. It is now shown that deposition of material from the fast transport system into membrane-associated structures, degradation of such deposited material and its return to the soma by the retrograde transport system, or leakage of radiolabeled material from the axon can account for the shape of the plateau. Furthermore, these processes are compatible with the maintenance of such structural inhomogeneities as the nodes of Ranvier.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060610
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  • 94
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    The origin of flagella-autogenous or symbiontic? (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 96-98 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; evolution ; eukaryotes ; phagotrophy ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Earlier hypotheses of the origin of flagella appear untenable in the light of recent evidence on the ancestry of eukaryotes. It is suggested that microtubules and flagella evolved early in eukaryote evolution to enhance phagotrophy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060205
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  • 95
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    Parameters of the ciliary cycle under membrane voltage control (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 89-95 
    Details
    ISSN: 0886-1544
    Keywords: Ciliary inclination ; bending reorientation ; power stroke ; ciliary amplitude ; angular velocity ; unipolar sliding transfer ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Axial views of depolarization- and hyperpolarization-dependent activation of the frontal cirri of Stylonychia were cinematically recorded at high rate (250 frames/s) under voltage-clamp. Images of a cirrus performing the cycle were processed by using computer assistance. In responding to the polarity and amplitude of the voltage signal, a cirrus inclines proximally with a particular angle and orientation. The ciliary cycle-always counterclockwise-is superimposing upon steady inclination. Correction for inclination allowed the assessment of the directional change rate and, after inclusion of the amplitude data, the determination of the ciliary angular velocity during the cycle. The method serves to isolate a new ciliary parameter: inclination, and to register precisely parameters of the cycle which may be meaningful for the understanding of the sliding mechanism.
    Additional Material: 5 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060204
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  • 96
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    Regulation of sperm flagellar movement by protein phosphorylation and dephosphorylation (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 83-88 
    Details
    ISSN: 0886-1544
    Keywords: sea urchin ; spermatozoa ; Triton model ; protein kinase ; cyclic AMP ; phosphoprotein phosphatase ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Flagellar motility of Triton models of sea urchin spermatozoa was reactivated by cyclic AMP-dependent protein kinase and a protein factor, termed motility activator, both of which were prepared from the detergent-extract of sea urchin spermatozoa. It was shown that phosphorylation of the motility activator by the protein kinase is necessary for the reactivation of flagellar motility [Ishiguro et al, J. Cell Biol. 92:777-782, 1982; Murofushi et al, in “Biological Functions of Microtubules and Related Structures,” Academic Press, 1982]. Reactivating factor was also detected in a KCI-extract of the axoneme fraction devoid of the detergent-extractable materials. The activity of this factor was also cyclic AMP- and protein kinase-dependent. Furthermore, when freshly prepared Triton models were treated with phosphoprotein phosphatase prepared from bovine cardiac muscle, the flagellar motility was drastically suppressed. This inhibition of the motility was partially recovered by the addition of cyclic AMP and protein kinase to the phosphatase-treated models.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/cm.970060203
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  • 97
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    Patterns of flagellar wave propagation in Crithidia oncopelti at increased viscosities (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 99-104 
    Details
    ISSN: 0886-1544
    Keywords: flagella ; wave shapes ; motility ; calcium ; adaptation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In its normal culturing environment, the trypanosomid flagellate Crithidia oncopelti propagates basally-directed planar waves, but may under certain conditions exhibit base-to-tip wave propagation in what is regarded as an avoidance response. The beat frequency and wave shape in both modes of beating are dependent on the viscosity of the swimming medium; viscosity may also influence the direction of wave propagation. If Crithidia experience a sudden increase in viscosity, there is a marked increase in the proportion of the population that is seen to exhibit wave propagation from base to tip; this proportion gradually decreases with time until the whole sample has reverted to “normal” beating. In a single organism, the resumption of normal beating is not accomplished in a single transition but by a series of switches between the forward and reverse modes. The interval of time between successive switches appears to be random, while the length of time spent in base-to-tip wave propagation gradually decreases. Despite the randomness of the switching process, its rate when averaged over successive time intervals is found to be constant at a particular viscosity and also dependent on it. The precise manner by which this organism is able to control its direction of wave propagation is unclear. However, the switching behavior it exhibits during the period of adaptation to an increased mechanical loading of the flagellum may reflect a process that characterizes a facet of this controlling mechanism.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060206
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  • 98
    Electronic Resource
    Electronic Resource
    Regulation of cell motility, morphology, and growth by sulfated glycosaminoglycans (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 273-281 
    Details
    ISSN: 0886-1544
    Keywords: heparin ; glycosaminoglycans ; fibronectin ; cell growth factors ; cell migration ; cell adhesion ; cell morphology ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Due to the recent observation that heparin binds to several growth factors and cell adhesion molecules, the effect of heparin on biological processes governed by growth factors and cell adhesion molecules was investigated. Pharmacological doses of heparin were found to alter cell growth rate, cellular morphology, and cell motility.Concentrations (μg/ml) of heparin or dextran sulfate decreased cell growth rate, but not the final cell density attained in plateau phase. The effect of heparin on cell growth rate was most pronounced when cells were cultured in low concentrations of serum. A heparin-induced decrease in cell growth rate could be reversed by addition of platelet-derived growth factor (PDGF), a heparin-binding growth factor.Heparin altered the morphology of all cell lines studied to various degrees. The effect of heparin on cell morphology was quantitated by measuring the heparin-induced change in cell surface area. HT-1080 and HeLa cells nearly doubled in surface area upon exposure to 10μg/ml heparin. Since several heparin-binding cell adhesion proteins mediate both cell spreading and cell migration, the influence of heparin on cell migration was investigated with an improved version of the phagokinetic track technique. Low concentrations of heparin and dextran sulfate were found to increase the rate of cell migration in a dose-dependent fashion.Since the quantitative effect of heparin on cell growth rate, morphology, and migration depends on the cell line studied, it is suggested that three separate phenomena may be involved. The results presented indicate a central role for sulfated glycosaminoglycans in the control of both cell growth and cell-cell interactions.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060304
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  • 99
    Electronic Resource
    Electronic Resource
    The stabilization of microtubules in isolated spindles by tubulin-colchicine complex (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 282-290 
    Details
    ISSN: 0886-1544
    Keywords: mitosis ; microtubules ; colchicine ; isolated mitotic spindles ; birefringence ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have analyzed the effect of colchicine and tubulin dimer-colchicine complex (T-C) on microtubule assembly in mitotic spindles. Cold- and calcium-labile mitotic spindles were isolated from embryos of the sea urchin Lytechinus variegatus employing EGTA/glycerol stabilization buffers. Polarization microscopy and measurements of spindle birefringent retardation (BR) were used to record the kinetics of microtubule assembly-disassembly in single spindles. When isolated spindles were perfused out of glycerol stabilizing buffer into a standard in vitro microtubule reassembly buffer (0.1 M Pipes, pH 6.8, 1 mM EGTA, 0.5 mM MgCl2, and 0.5 mM GTP) lacking glycerol, spindle BR decreased with a halftime of 120 s. Colchicine at 1 mM in this buffer had no effect on the rate of spindle microtubule disassembly. Inclusion of 20 μM tubulin or microtubule protein, purified from porcine brain, in this buffer resulted in an augmentation of spindle BR. Interestingly, in the presence of 20 μM T-C, spindle BR did not increase, but was reversibly stabilized; subsequent perfusion with reassembly buffer without T-C resulted in depolymerization. This behavior is striking in contrast to the rapid depolymerization of spindle microtubules induced by colchicine and T-C in vivo. These results support the current view that colchicine does not directly promote microlubule depolymerization. Rather, it is T-C complex that alters microtubule assembly, by reversibly binding to microtubules and inhibiting elongation.In vivo, colchicine can induce depolymerization of nonkinetochore spindle microtubules within 20 s. In vitro, colchicine blocks further microtubule assembly, but does not induce rapid disassembly. The rate of tubulin dissociation from spindle microtubules in vitro in reassembly buffer without soluble tubulin is about 20 times slower than the rate of dissociation in vivo when assembly is blocked abruptly by T-C. The rate of tubulin dissociation from the spindle microtubules may determine their response to T-C, since the tubulin dissociation rate in vivo is about 12 times faster than the rate measured here for spindle microtubules in standard microtubule reassembly buffer at physiological temperature.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060305
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  • 100
    Electronic Resource
    Electronic Resource
    Effects of vanadate on the assembly and disassembly of purified tubulin (1986)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 6 (1986), S. 314-323 
    Details
    ISSN: 0886-1544
    Keywords: vanadate ; microtubules ; tubulin polymerization ; taxol ; dynein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Sodium-orthovanadate (100-700 μM) added to purified pig brain microtubule protein (molar ratios 13-90 moles vanadate/mole tubulin) inhibits to a considerable extent the assembly (up to 65%) and the disassembly rates (up to 60%) of microtubules, as determined by turbidimetry. Vanadate added to preformed microtubules did not appreciably alter the turbidity level of the samples, however, the disassembly rates were decreased in the same manner as when vanadate was added prior to polymerization. Microtubule protein kept on ice for 3-6 hours became more susceptible to vanadate than freshly prepared protein. The effect of vanadate was independent of the GTP concentration at which the polymerization assays were performed (0.025 to 1 mM GTP). In the presence of taxol, which increases the rate and extent of microtubule formation, vanadate had no effect on assembly rates. Disassembly was inhibited, however, much less than in the presence of vanadate alone. Electron microscopy and polyacrylamide gel electrophoresis did not reveal differences between microtubules prepared in the presence or in the absence of vanadate. This is consistent with the notion that vanadate does not interfere with the interaction between tubulin and the high-molecular weight microtubule-associated proteins. Apparently vanadate brings about an allosteric change of the microtubule protein(s) resulting in the abnormal polymerization kinetics of tubulin found in our study. The above results may be relevant for studies where the effects of vanadate on intracellular motility are interpreted as being solely due to a specific inhibition of ATPases.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970060308
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