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  • 1985-1989  (2)
  • microtubule  (1)
  • α chain  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Tubulin tyrosination in Crithidia: Modifying enzymes and modification states of tubulin (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 10 (1988), S. 400-409 
    Details
    ISSN: 0886-1544
    Keywords: C-terminal tyrosine ; flagellar α chain ; α chain ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: An enzyme that adds C-terminal tyrosine to tubulin has been identified in Crithidia fasciculata. It tyrosinates Crithidia, but not brain, tubulin and is specific for the α chain. Crithidia cells could not be shown to fix tyrosine in the absence of protein synthesis, which is consistent with the pattern of distribution of C-terminal tyrosine in tubulin from different subcellular compartments of this protozoan. Terminal tyrosine was present in about 5% of flagellar α chain from cells in stationary phase and 20% from cells from midlog phase; none was detected in tubulin from cytosol or the subpellicular corset. In contrast to mammalian cells, in which a higher state of tyrosinolation characterizes recently assembled or unstable microtubules, terminal tyrosine was present only in the most stable polymer, the flagellar doublet microtubules.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970100307
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical studies with antibodies to three proteins prominent in the isolated microtubule cytoskeleton of a trypanosomatid (1989)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 13 (1989), S. 145-157 
    Details
    ISSN: 0886-1544
    Keywords: microtubule ; membrane ; sytoskeleton ; Trypanosomatidae ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The cytoskeleton of Crithidia fasciculata consists of a corset of paralle microtubules enclosing the cell body and closely underlying the plasma membrane. Distinct sets of crosslinks appear to connect tubules to each other and to membrane. Our objective is to determine the composition of these crosslinks and to elucidate the basis of this spectacular example of membrane-microtubule interaction. We purified three proteins (designated COP-33, -41, and -61 by their subunit Mr), which were consistently abundant in highly purified cytoskeletons. All three bound strongly to microtubules in vitro, and the first two induced bundles through periodic crosslinking. Polyclonal antibodies against each have been used to try to localize these proteins in thin sections of cells or whole mounts of cytoskeletons. Antibodies to COP-41 bound sepcifically to glycosomes, organelles that encapsulate many glycolytic enzymes in these protozoa, and COP-41 has been identified as glyceraldehyde 3-P dehydrogenase.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970130303
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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