Phosphorylation of Sic1p by G1 Cdk Required for Its Degradation and Entry into S Phase

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摘要：

G1 cyclin-dependent kinase (Cdk)-triggered degradation of the S-phase Cdk inhibitor Sic1p has been implicated in the transition from G1 to S phase in the cell cycle of budding yeast. A multidimensional electrospray mass spectrometry technique was used to map G1 Cdk phosphorylation sites in Sic1p both in vitro and in vivo. A Sic1p mutant lacking three Cdk phosphorylation sites did not serve as a substrate for Cdc34p-dependent ubiquitination in vitro, was stable in vivo, and blocked DNA replication. Moreover, purified phosphoSic1p was ubiquitinated in cyclin-depleted G1 extract, indicating that a primary function of G1 cyclins is to tag Sic1p for destruction. These data suggest a molecular model of how phosphorylation and proteolysis cooperate to bring about the G1/S transition in budding yeast.

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Amino Acid Sequence Chimeric Proteins metabolism Cyclin-Dependent Kinases metabolism Cyclins metabolism DNA Replication Enzyme Inhibitors metabolism Fungal Proteins metabolism G1 Phase Ligases metabolism Molecular Sequence Data Mutagenesis Phenotype Phosphopeptides metabolism Phosphorylation Research Support Non-U.S. Gov't Research Support U.S. Gov't P.H.S. S Phase Saccharomyces cerevisiae Proteins Ubiquitin-Protein Ligase Complexes Ubiquitin-Protein Ligases Ubiquitins metabolism Yeasts cytology metabolism