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Department of Physiology, University of California, San Francisco,
California 94143-0444
Exit from mitosis requires the inactivation of mitotic
cyclin-dependent kinase-cyclin complexes, primarily by
ubiquitin-dependent cyclin proteolysis. Cyclin destruction is regulated
by a ubiquitin ligase known as the anaphase-promoting complex (APC). In
the budding yeast Saccharomyces cerevisiae, members of a
large class of late mitotic mutants, including cdc15,
cdc5, cdc14, dbf2, and
tem1, arrest in anaphase with a phenotype similar to
that of cells expressing nondegradable forms of mitotic cyclins. We
addressed the possibility that the products of these genes are
components of a regulatory network that governs cyclin proteolysis. We
identified a complex array of genetic interactions among these mutants
and found that the growth defect in most of the mutants is suppressed
by overexpression of SPO12, YAK1, and
SIC1 and is exacerbated by overproduction of the mitotic
cyclin Clb2. When arrested in late mitosis, the mutants exhibit a
defect in cyclin-specific APC activity that is accompanied by high Clb2
levels and low levels of the anaphase inhibitor Pds1. Mutant cells
arrested in G1 contain normal APC activity. We conclude that Cdc15,
Cdc5, Cdc14, Dbf2, and Tem1 cooperate in the activation of the APC in
late mitosis but are not required for maintenance of that activity in
G1.
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