The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20.
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.
Mesh Terms:
Adenosine Triphosphate, Cell Cycle Proteins, Chaperonin Containing TCP-1, Chaperonins, Chromosome Segregation, Evolution, Molecular, Genes, cdc, Hydrolysis, Ligases, Mitosis, Protein Binding, Protein Folding, Protein Structure, Tertiary, Ubiquitin-Protein Ligase Complexes, Yeasts
Adenosine Triphosphate, Cell Cycle Proteins, Chaperonin Containing TCP-1, Chaperonins, Chromosome Segregation, Evolution, Molecular, Genes, cdc, Hydrolysis, Ligases, Mitosis, Protein Binding, Protein Folding, Protein Structure, Tertiary, Ubiquitin-Protein Ligase Complexes, Yeasts
Mol. Cell
Date: Jul. 01, 2003
PubMed ID: 12887895
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