Abstract：
:Cyclin B is degraded at the onset of anaphase by a ubiquitin-dependent proteolytic system. We have fractionated mitotic Xenopus egg extracts to identify components required for this process. We find that UBC4 and at least one other ubiquitin-conjugating enzyme can support cyclin B ubiquitination. The mitotic specificity of cyclin ubiquitination is determined by a 20S complex that contains homologs of budding yeast CDC16 and CDC27. Because these proteins are required for anaphase in yeast and mammalian cells, we refer to this complex as the anaphase-promoting complex (APC). CDC27 antibodies deplete APC activity, while immunopurified CDC27 complexes are sufficient to complement either interphase extracts or a mixture of recombinant UBC4 and the ubiquitin-activating enzyme E1. These results suggest that APC functions as a regulated ubiquitin-protein ligase that targets cyclin B for destruction in mitosis.
journal_name
Celljournal_title
Cellauthors
King RW,Peters JM,Tugendreich S,Rolfe M,Hieter P,Kirschner MWdoi
10.1016/0092-8674(95)90338-0subject
Has Abstractpub_date
1995-04-21 00:00:00pages
279-88issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(95)90338-0journal_volume
81pub_type
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