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and
*Department of Microbiology, Keio University School of
Medicine, Tokyo 160-8582, Japan; and
In the yeast Saccharomyces cerevisiae, Sic1, an
inhibitor of Clb-Cdc28 kinases, must be phosphorylated and degraded in
G1 for cells to initiate DNA replication, and Cln-Cdc28
kinase appears to be primarily responsible for phosphorylation of Sic1.
The Pho85 kinase is a yeast cyclin-dependent kinase (Cdk), which is not essential for cell growth unless both CLN1 and
CLN2 are absent. We demonstrate that Pho85, when
complexed with Pcl1, a G1 cyclin homologue, can
phosphorylate Sic1 in vitro, and that Sic1 appears to be more stable in
pho85Department of
Biological Sciences, Graduate School of Science, The University of
Tokyo, Tokyo 113-0033, Japan
cells. Three consensus Cdk phosphorylation sites present in Sic1 are phosphorylated in vivo, and two of them are
required for prompt degradation of the inhibitor. Pho85 and other
G1 Cdks appear to phosphorylate Sic1 at different sites in
vivo. Thus at least two distinct Cdks can participate in
phosphorylation of Sic1 and may therefore regulate progression through
G1.
Corresponding author. E-mail address:
mas{at}mc.med.keio.ac.jp.
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