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.
Camasses
Alain
A
Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany.
Bogdanova
Aliona
A
Shevchenko
Andrej
A
Zachariae
Wolfgang
W
D000255:Adenosine Triphosphate / Q000378:metabolism; D064173:Anaphase-Promoting Complex-Cyclosome; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins / Q000235:genetics / Q000378:metabolism*; D020090:Chromosome Segregation / Q000235:genetics; D019143:Evolution, Molecular; D018816:Genes, cdc / Q000502:physiology; D006868:Hydrolysis; D008025:Ligases / Q000235:genetics / Q000378:metabolism*; D008938:Mitosis / Q000235:genetics*; D011485:Protein Binding / Q000502:physiology; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000235:genetics; D043743:Ubiquitin-Protein Ligase Complexes; D015003:Yeasts / Q000235:genetics / Q000378:metabolism*
D018797:Cell Cycle Proteins; D000255:Adenosine Triphosphate; D043743:Ubiquitin-Protein Ligase Complexes; D064173:Anaphase-Promoting Complex-Cyclosome; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins; D008025:Ligases