The effect of chaperonin buffering on protein evolution

Genome Biology and Evolution
Tom A Williams, Mario A Fares

Abstract

Molecular chaperones are highly conserved and ubiquitous proteins that help other proteins in the cell to fold. Pioneering work by Rutherford and Lindquist suggested that the chaperone Hsp90 could buffer (i.e., suppress) phenotypic variation in its client proteins and that alternate periods of buffering and expression of these variants might be important in adaptive evolution. More recently, Tokuriki and Tawfik presented an explicit mechanism for chaperone-dependent evolution, in which the Escherichia coli chaperonin GroEL facilitated the folding of clients that had accumulated structurally destabilizing but neofunctionalizing mutations in the protein core. But how important an evolutionary force is chaperonin-mediated buffering in nature? Here, we address this question by modeling the per-residue evolutionary rate of the crystallized E. coli proteome, evaluating the relative contributions of chaperonin buffering, functional importance, and structural features such as residue contact density. Previous findings suggest an interaction between codon bias and GroEL in limiting the effects of misfolding errors. Our results suggest that the buffering of deleterious mutations by GroEL increases the evolutionary rate of client proteins...Continue Reading

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Methods Mentioned

BETA
protein folding

Related Concepts

Bacterial Proteins
Alkalescens-Dispar Group
Mycoplasma putrefaciens
Protein Folding, Globular
Chaperonin Complexes
GroEL Protein
Evolution, Molecular
Proteome
Escherichia coli Proteins
Buffers

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