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Fission yeast cyclin: subcellular localisation and cell cycle regulation
Journal of Cell Science. Supplement
|January 1, 1989
Summary
Fission yeast cdc13 protein acts like a classic cyclin, accumulating during interphase and degrading at mitosis. It is essential for localizing the cdc2 protein to the nucleus in Schizosaccharomyces pombe.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Entry into mitosis is regulated by interactions between cell cycle control genes.
- cdc2+ is a major cell cycle control gene in fission yeast.
- cdc13+ encodes a protein homologous to cyclin.
Purpose of the Study:
- To investigate the localization and cell cycle behavior of cdc13 and cdc2 proteins in Schizosaccharomyces pombe.
- To determine the functional relationship between cdc13 and cdc2 in nuclear localization.
Main Methods:
- Indirect immunofluorescence microscopy using antibodies against bacterially-expressed proteins.
- Analysis of protein localization and levels in wild-type and gene-disrupted fission yeast strains.
Main Results:
- Both cdc13 and cdc2 are nuclear proteins in S. pombe, localized to a domain distinct from chromatin.
- cdc13 and cdc2 levels increase during interphase and decrease at mitosis (cdc13 is degraded, cdc2 remains constant).
- Disruption of cdc13+ prevents nuclear accumulation of both cdc13 and cdc2, while disruption of cdc2+ affects cdc2 but not cdc13 nuclear levels.
Conclusions:
- cdc13 functions as a classic cyclin, undergoing degradation at mitosis.
- cdc13 is required for the nuclear localization of cdc2 in S. pombe.
- cdc2 does not appear to be required for cdc13 nuclear localization, suggesting a unidirectional regulatory role.