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  • Articles: DFG German National Licenses  (2)
  • Adenylate cyclase  (1)
  • Basal-body root complex  (1)
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  • Articles: DFG German National Licenses  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    A monoclonal antibody to animal centrosomes recognizes components of the basal-body root complex inChlamydomonas (1990)
    Springer
    Protoplasma 153 (1990), S. 208-211 
    Details
    ISSN: 1615-6102
    Keywords: Basal-body root complex ; Cell division cycle ; Centrosome ; Chlamydomonas ; Evolution ; Monoclonal antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The mammalian centrosome monoclonal antibody MPM-13 recognized component(s) of the well defined MTOC basal-body root complex in the green plantChlamydomonas. The antibody reaction coincided in location with the basal-body root complex and the cruciate nature of the staining pattern corresponded to the configuration of the root microtubules. During mitosis the behaviour of MPM-13 stained material mirrored the duplication, separation and migration to the spindle poles of the basal body-root complex. It is suggested that conserved MTOC components were recognized and that these may have retained a similar, perhaps universal, function in microtubule organization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01354006
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Temperature conditional cAMP-requiring mutant strains ofChlamydomonas reinhardtii arrest in G1 and are rescued by added cAMP (1996)
    Springer
    Protoplasma 192 (1996), S. 159-167 
    Details
    ISSN: 1615-6102
    Keywords: Adenylate cyclase ; Cell cycle ; Chlamydomonas reinhardtii ; Cyclic AMP ; Cyclic nucleotide phosphodiesterase ; Mutant strains
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Three independent isolates ofChlamydomonas, selected for caffeine resistance, were found to arrest in G1 phase, as determined by quantitative fluorescence measurements of DNA, when grown at a non-permissive temperature. This cell cycle arrest correlated with lowered levels of cAMP and of adenylate cyclase activity. The arrested cells could be rescued by added cAMP but not AMP, hence the defect was not one of general purine metabolism. Back-crosses to wild type revealed that the phenotypes observed result from a combination of three separable mutations. It is clear that the mutations define functions that are more stringently required for cell division than for growth since the mutant strains are able to grow up to fifteen times normal size while blocked at the non-permissive temperature. The possible interaction of cAMP dependent events with division is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01273888
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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