A 20s complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B

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. Th...

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Bibliographic Details
Published in:Cell 1995-04, Vol.81 (2), p.279-288
Main Authors: King, Randall W, Peters, Jan-Michael, Tugendreich, Stuart, Rolfe, Mark, Hieter, Philip, Kirschner, Marc W
Format: Article
Language:English
Subjects:
Anaphase - physiology
Animals
Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome
Apc6 Subunit, Anaphase-Promoting Complex-Cyclosome
Cell Cycle Proteins - metabolism
Cyclins - metabolism
Freshwater
Ligases - analysis
Ligases - genetics
Ligases - metabolism
Macromolecular Substances
Mitosis - physiology
Ovum
Recombinant Proteins - pharmacology
Saccharomyces cerevisiae Proteins
Subcellular Fractions - metabolism
Ubiquitin-Activating Enzymes
Ubiquitin-Conjugating Enzymes
Ubiquitin-Protein Ligases
Ubiquitins - metabolism
Xenopus
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Summary: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.
ISSN:0092-8674
1097-4172
DOI:10.1016/0092-8674(95)90338-0