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Linkage of replication to start by the Cdk inhibitor Sic1.

Science (New York, N.Y.) | Apr 26, 1996

In Saccharomyces cerevisiae, three G1 cyclins (Clns) are important for Start, the event committing cells to division. Sic1, an inhibitor of C1b-Cdc28 kinases, became phosphorylated at Start, and this phosphorylation depended on the activity of Clns. Sic1 was subsequently lost, which depended on the activity of Clns and the ubiquitin-conjugating enzyme Cdc34. Inactivation of Sic1 was the only nonredundant essential function of Clns, because a sic1 deletion rescued the inviability of the cln1 cln2 cln3 triple mutant. In sic1 mutants, DNA replication became uncoupled from budding. Thus, Sic1 may be a substrate of Cln-Cdc28 complexes, and phosphorylation and proteolysis of Sic1 may regulate commitment to replication at Start.

Pubmed ID: 8614808 RIS Download

Mesh terms: Anaphase-Promoting Complex-Cyclosome | CDC28 Protein Kinase, S cerevisiae | Cell Cycle | Cyclin-Dependent Kinase Inhibitor Proteins | Cyclins | DNA Replication | DNA, Fungal | Enzyme Inhibitors | Fungal Proteins | Ligases | Phosphorylation | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Ubiquitin-Conjugating Enzymes | Ubiquitin-Protein Ligase Complexes | Ubiquitin-Protein Ligases

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM39978

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