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Vol. 10, Issue 4, 833-845, April 1999
Departments of Molecular Biology and Cell Biology, The
Scripps Research Institute, La Jolla, California 92037
In the fission yeast Schizosaccharomyces pombe, the
protein kinase Cds1 is activated by the S-M replication checkpoint
that prevents mitosis when DNA is incompletely replicated. Cds1 is proposed to regulate Wee1 and Mik1, two tyrosine kinases that inhibit
the mitotic kinase Cdc2. Here, we present evidence from in vivo and in
vitro studies, which indicates that Cds1 also inhibits Cdc25, the
phosphatase that activates Cdc2. In an in vivo assay that measures the
rate at which Cdc25 catalyzes mitosis, Cds1 contributed to a mitotic
delay imposed by the S-M replication checkpoint. Cds1 also inhibited
Cdc25-dependent activation of Cdc2 in vitro. Chk1, a protein kinase
that is required for the G2-M damage checkpoint that
prevents mitosis while DNA is being repaired, also inhibited Cdc25 in
the in vitro assay. In vitro, Cds1 and Chk1 phosphorylated Cdc25
predominantly on serine-99. The Cdc25 alanine-99 mutation partially
impaired the S-M replication and G2-M damage checkpoints
in vivo. Thus, Cds1 and Chk1 seem to act in different checkpoint
responses to regulate Cdc25 by similar mechanisms.
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