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  • 1
    Electronic Resource
    Electronic Resource
    Immunological Characterization of Trichocyst Proteins In the Ciliate Pseudomicrothorax Dubius (1993)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 40 (1993), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: . Ejectable trichocysts were isolated from the ciliate Pseudomicrothorax dubius. Polyclonal antibodies were raised against three groups of trichocyst proteins: G1 (30-31 kDa), G2 (26-27 kDa) and G3 (15-20 kDa). By indirect immunofluorescence, the three antisera strongly label the shafts of ejected trichocysts and the proximal ends of condensed trichocysts within the cells. By immunogold labeling for electron microscopy, the three sera specifically recognize the shafts of both extended and condensed trichocysts and shaft precursors in pretrichocysts as well. On one-dimensional immunoblots of isolated trichocysts, anti-G1 serum recognizes the G1 proteins, anti-G2 serum detects G2 proteins and some G1 proteins, and anti-G3 serum reacts with 15 bands, mainly the G3 and (30-41)-kDa proteins. In cells with and without trichocysts, the sera recognize non-ejectable trichocyst proteins at 41-42 kDa and 47 kDa. On two-dimensional immunoblots of isolated trichocysts, anti-G1 serum labels proteins with a pI of 4.75-5.7, anti-G2 serum labels proteins with a pI of 4.75-6.25 and anti-G3 serum labels proteins with a pI of 4.7-6.6. Analyses of cells with and without trichocysts allow identification of possible precursors between 41 and 47 kDa. Some are in the same pI range as their putative products, but others, labeled by anti-G3 serum, are less acidic than most of their mature products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1993.tb04886.x
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  • 2
    Electronic Resource
    Electronic Resource
    Biochemical Study of Proteins of Cortical Cytoskeleton in the Ciliate Isotricha prostoma (1985)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 32 (1985), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: In Isotricha prostoma, proteins of isolated cortices retaining the ecto-endoplasmic fibrillar boundary (EEB) have been separated by one- and two-dimensional gel electrophoresis. In addition to that of tubulin, four main bands corresponding to polypeptide molecular weights of 185, 35, 23, and 22 kd have been observed on 9% SDS-polyacrylamide gels. Supernumerary major bands within a low molecular weight range (11-19 kd) are evident after separation on 7.5-15% polyacrylamide gradient gels. Two-dimensional analysis discloses - 150 polypeptide spots, most of them focusing within an acidic pl range 4.6-5.3. The cortical fibrillar structures are still distinguishable after incubation in solutions containing 1.0 M K. Cl (12 h) or 0.6 M Kl (8 h). A prolonged KI treatment (52 h), however, results in the removal of EEB filaments (˜4 nm in diameter) and of a large part of the kinetid elements, so that the insoluble material is mainly represented by a reticulum of 6-nm filaments interconnecting the proximal regions of kinetosomes. Two proteins with MW of 58 and 63 kd appear to be constituents of this kinetosome-associated filamentous reticulum. Some of the cortical proteins with MW ≤23 kd are the most likely candidates for components of EEB filaments. The absence of decoration with heavy meromyosin confirms that actin is not a major component of Isotricha cortical cytoskeleton.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1985.tb03010.x
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  • 3
    Electronic Resource
    Electronic Resource
    Calmyonemin: A 23 kDa analogue of algal centrin occurring in contractile myonemes of Eudiplodinium maggii (ciliate) (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 27 (1994), S. 169-179 
    Details
    ISSN: 0886-1544
    Keywords: calcium-binding proteins ; myonemes ; centrin ; contractility ; ciliates ; protozoa ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Myonemes are bundles of thin filaments (3-6 nm in diameter) which mediate calcium-induced contraction of the whole or only parts of the cell body in a number of protists. In Eudiplodinium maggii, a rumen ciliate which lacks a uniform ciliation of the cell body, myonemes converge toward the bases of apical ciliary zones that can be retracted under stress conditions, entailing immobilization of the cell. An mAB (A69) has been produced that identifies a calciumbinding protein by immunoblot, immunoprecipitation experiments and specifically labels the myonemes in immunoelectron microscopy. Solubility properties, apparent molecular weight (23 kDa) and isoelectric point (4.9) of the myonemal protein, are similar to the values reported for the calcium-modulated contractile protein centrin. Western-blot analysis indicates that the 23 kDa protein crossreacts antigenically with anti-centrin antibodies. In addition, the 23 kDa protein displays calcium-induced changes in both electrophoretic and chromatographic behaviour, and contains calcium-binding domains that conform to the EF-hand structure, as known for centrin. Based on these observations, we conclude that a calcium-binding protein with major similarities to centrin occurs in the myonemes of E. maggii. We postulate that this protein plays an essential role in myonememediated retraction of the ciliature. © 1994 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970270208
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