Abstract
The WD repeat protein Cdc20 is essential for progression through mitosis because it is required to activate ubiquitin ligation by the anaphase-promoting complex (APC/C). Here we show in yeast that Cdc20 binds to the CCT chaperonin, which is known as a folding machine for actin and tubulin. The CCT is required for Cdc20's ability to bind and activate the APC/C. In vivo, CCT is essential for Cdc20-dependent cell cycle events such as sister chromatid separation and exit from mitosis. The chaperonin is also required for the function of the Cdc20-related protein Cdh1, which activates the APC/C during G1. We propose that folding of the Cdc20 family of APC/C activators is an essential and evolutionary conserved function of the CCT chaperonin.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism
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Anaphase-Promoting Complex-Cyclosome
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Cell Cycle Proteins / genetics
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Cell Cycle Proteins / metabolism*
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Chaperonin Containing TCP-1
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Chaperonins / genetics
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Chaperonins / metabolism*
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Chromosome Segregation / genetics
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Evolution, Molecular
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Genes, cdc / physiology
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Hydrolysis
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Ligases / genetics
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Ligases / metabolism*
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Mitosis / genetics*
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Protein Binding / physiology
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Protein Folding
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Protein Structure, Tertiary / genetics
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Ubiquitin-Protein Ligase Complexes*
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Yeasts / genetics
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Yeasts / metabolism*
Substances
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Cell Cycle Proteins
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Adenosine Triphosphate
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Ubiquitin-Protein Ligase Complexes
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Anaphase-Promoting Complex-Cyclosome
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Chaperonin Containing TCP-1
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Chaperonins
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Ligases