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  • Artikel: DFG Deutsche Nationallizenzen  (2)
  • Cytoskeleton  (2)
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  • Artikel: DFG Deutsche Nationallizenzen  (2)
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  • 1
    ISSN: 1615-6102
    Schlagwort(e): Algae ; Cytoskeleton ; Microtubules ; Microtubule organizing centres ; Mutation ; Temperature-sensitive
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary We have isolated a number of temperature conditional cell division cycle mutants of the unicellular plantChlamydomonas reinhardtii that are defective in single nuclear genes. Cells grow and divide normally at the permissive temperature (21 °C), but arrest in division at the restrictive temperature (33 °C). We have characterized these mutants using DNA probes and immunofluorescence techniques to localize cytoskeletal and microtubule organizing centre proteins. We describe here 3 broad classes of cell cycle mutation which result in cell cycle arrest with: unreplicated DNA (G1 arrest), duplicated DNA (G2 arrest) and multiple nuclei due to defective cytokinesis (cytokinesis arrest). The continuation of nuclear division in mutants blocked in cytokinesis provides support of an earlier hypothesis that stage specific events in theChlamydomonas cell cycle are arranged in separate dependent sequences. The mutants isolated in the present study provide insights into the role of cytoskeletal proteins in the coordination of plant cell division and the means to investigate the molecular mechanisms whereby division by multiple fission is controlled in the unicellular plantChlamydomonas.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1615-6102
    Schlagwort(e): Centrin ; Chilomastix cuspidata ; Cytoskeleton ; Protist ; Tubulin ; Retortamonad
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Immunochemical techniques were used to identify and localise centrin and α-tubulin inChilomastix cuspidata, an amitochondriate “excavate flagellate”. Immunoblotting showed that the molecular mass of centrin is 20 kDa and α-tubulin is 55 kDa. Immunofluorescence microscopy localises centrin to the basal-body region of the flagellar apparatus and in a centrin-containing root which runs along the groove towards the posterior of the cell. Confocal microscopy of cells double-labelled with anticentrin and antitubulin antibodies suggests that centrin is also associated with a group of microtubules called the hook band. Centrin labelling extends for two thirds of the length of the hook band, ending in a pill-like structure. In all we distinguish five major components of the centrin root. The distribution of these proteins is discussed in terms of the functions centrin and tubulin may play in this putatively primitive protist and its relatives.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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