The Molecular Chaperone DnaK Is a Source of Mutational Robustness

Genome Biology and Evolution
Jose Aguilar-RodriguezMario A Fares


Molecular chaperones, also known as heat-shock proteins, refold misfolded proteins and help other proteins reach their native conformation. Thanks to these abilities, some chaperones, such as the Hsp90 protein or the chaperonin GroEL, can buffer the deleterious phenotypic effects of mutations that alter protein structure and function. Hsp70 chaperones use a chaperoning mechanism different from that of Hsp90 and GroEL, and it is not known whether they can also buffer mutations. Here, we show that they can. To this end, we performed a mutation accumulation experiment in Escherichia coli, followed by whole-genome resequencing. Overexpression of the Hsp70 chaperone DnaK helps cells cope with mutational load and completely avoid the extinctions we observe in lineages evolving without chaperone overproduction. Additionally, our sequence data show that DnaK overexpression increases mutational robustness, the tolerance of its clients to nonsynonymous nucleotide substitutions. We also show that this elevated mutational buffering translates into differences in evolutionary rates on intermediate and long evolutionary time scales. Specifically, we studied the evolutionary rates of DnaK clients using the genomes of E. coli, Salmonella enter...Continue Reading


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Datasets Mentioned


Methods Mentioned

nucleotide exchange
restriction digest

Related Concepts

DnaK protein, E coli
Alkalescens-Dispar Group
Point Mutation
Heat-Shock Proteins 70
Escherichia coli Proteins
Base Sequence
Escherichia coli
Biological Evolution
Heat shock proteins

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