Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.

Journal of the Royal Society, Interface
Gabriel M Altschuler, K R Willison

Abstract

A free-energy-based approach is used to describe the mechanism through which chaperonin-containing TCP-1 (CCT) folds the filament-forming cytoskeletal protein actin, which is one of its primary substrates. The experimental observations on the actin folding and unfolding pathways are collated and then re-examined from this perspective, allowing us to determine the position of the CCT intervention on the actin free-energy folding landscape. The essential role for CCT in actin folding is to provide a free-energy contribution from its ATP cycle, which drives actin to fold from a stable, trapped intermediate I3, to a less stable but now productive folding intermediate I2. We develop two hypothetical mechanisms for actin folding founded upon concepts established for the bacterial type I chaperonin GroEL and extend them to the much more complex CCT system of eukaryotes. A new model is presented in which CCT facilitates free-energy transfer through direct coupling of the nucleotide hydrolysis cycle to the phases of actin substrate maturation.

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Citations

Apr 25, 2012·Protoplasma·Julie GranthamRoger Karlsson
Nov 9, 2010·The Journal of Biological Chemistry·Sarah F StuartKeith R Willison
Jun 4, 2010·Bioinformatics·Emanuele RaineriTobias Maier
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Jan 26, 2010·Progress in Biophysics and Molecular Biology·Konstantin K TuroverovVladimir N Uversky
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Dec 14, 2012·Journal of the Royal Society, Interface·Jasmina Panovska-GriffithsJames Briscoe
Aug 15, 2014·Intrinsically Disordered Proteins·Olga I PovarovaKonstantin K Turoverov
Dec 17, 2009·Journal of Proteome Research·Chin-Chen ChuShung-Tai Ho
Aug 14, 2020·Journal of Agricultural and Food Chemistry·Xue ZhangMark Wesley Schilling

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