Characterization of fission yeast cohesin: essential anaphase proteolysis of Rad21 phosphorylated in the S phase
Article Abstract:
Fission yeast cohesin and essential anaphase proteolysis of S phase-phosphorylated Rad21 are discussed. Characterization of four putative cohesin subunits, needed for sister chromatid cohesion, Pac3, Psm1, Psm3, and Rad21 in fission yeast has been carried out for the first time. A simple model for explaining behvaior of fission yeast cohesin has been developed. It also gives an explanation for why a tiny fraction of Rad21 cleaved for normal anaphase is enough.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2000
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Whose end is destruction: cell division and the anaphase-promoting complex
Article Abstract:
The anaphase-promoting complex or cyclosome (APC/C), which was discovered four years ago, and cell division are discussed with a summary of available information about (APC/C) roles and regulation. By destroying anaphase inhibitory proteins, the APC/C brings on separation of sister chromatids, and by destroying mitotic cyclins, it sets up the low CDK state necessary for cytokinesis and for reforming the pre-RCs complexes needed for the next round of genome replication.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
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Fission yeast condensin complex: essential roles of non-SMC subunits for condensation and Cdc2 phosphorylation of Cut3/SMC4
Article Abstract:
Fission yeast condensin complex is discussed relative to essential roles of non-structural maintenance of chromosomes (SMC) subunits for Cdc2 phosphorylation and condensation of Cut3/SMC4. Fission yeast has the same five-member condensin complex as the condensin complex in frog extracts, which contains two SMC and three non-SMC subunits, with each of the five members essential for mitotic condensation. Direct phosphorylation of fission yeast condensin may aid in its nuclear accumulation during mitosis.
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1999
User Contributions:
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