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Vol. 8, Issue 10, 1877-1887, October 1997
Departments of
B-type cyclins are rapidly degraded at the transition between
metaphase and anaphase and their ubiquitin-mediated proteolysis is
required for cells to exit mitosis. We used a novel enrichment to
isolate new budding mutants that arrest the cell cycle in mitosis. Most
of these mutants lie in the CDC16, CDC23, and
CDC27 genes, which have already been shown to play a
role in cyclin proteolysis and encode components of a 20S complex
(called the cyclosome or anaphase promoting complex) that ubiquitinates
mitotic cyclins. We show that mutations in CDC26 and a
novel gene, DOC1, also prevent mitotic cyclin
proteolysis. Mutants in either gene arrest as large budded cells with
high levels of the major mitotic cyclin (Clb2) protein at 37°C and
cannot degrade Clb2 in G1-arrested cells. Cdc26 associates
in vivo with Doc1, Cdc16, Cdc23, and Cdc27. In addition, the majority
of Doc1 cosediments at 20S with Cdc27 in a sucrose gradient, indicating
that Cdc26 and Doc1 are components of the anaphase promoting complex.
Physiology and
*Biochemistry and
Biophysics, University of California, San Francisco, California
94143-0444
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