FEBS Letters
Volume 584, Issue 3 , Pages 477-481, 5 February 2010

On the role of the chaperonin CCT in the just-in-time assembly process of APC/CCdc20

Edited by Angel Nebreda

Cell and Molecular Biology, The Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, United Kingdom

Received 2 October 2009; received in revised form 16 November 2009; accepted 25 November 2009. published online 30 November 2009.

Abstract 

The just-in-time hypothesis relates to the assembly of large multi-protein complexes and their regulation of activation in the cell. Here I postulate that chaperonins may contribute to the timely assembly and activation of such complexes. For the case of anaphase promoting complex/cyclosomeCdc20 assembly by the eukaryotic chaperonin chaperonin containing Tcp1 it is shown that just-in-time synthesis and chaperone-assisted folding can synergise to generate a highly regulated assembly process of a protein complex that is vital for cell cycle progression. Once dependency has been established transcriptional regulation and chaperonin-dependency may have co-evolved to safeguard the timely activation of important multi-protein complexes.

Keywords: Chaperonin, CCT, APC/C, Just-in-time-assembly

Abbreviations: APC/C, anaphase promoting complex/cyclosome, CCT, chaperonin containing Tcp1, YMC, yeast metabolic cycle, PP2A, protein phosphatase 2A complex, TFIID, transcription factor II D complex

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PII: S0014-5793(09)01028-X

doi:10.1016/j.febslet.2009.11.088

FEBS Letters
Volume 584, Issue 3 , Pages 477-481, 5 February 2010