DnaK-Dependent Accelerated Evolutionary Rate in Prokaryotes

Genome Biology and Evolution
A Samer KadibalbanTal Dagan

Abstract

Many proteins depend on an interaction with molecular chaperones in order to fold into a functional tertiary structure. Previous studies showed that protein interaction with the GroEL/GroES chaperonine and Hsp90 chaperone can buffer the impact of slightly deleterious mutations in the protein sequence. This capacity of GroEL/GroES to prevent protein misfolding has been shown to accelerate the evolution of its client proteins. Whether other bacterial chaperones have a similar effect on their client proteins is currently unknown. Here, we study the impact of DnaK (Hsp70) chaperone on the evolution of its client proteins. Evolutionary parameters were derived from comparison of the Escherichia coli proteome to 1,808,565 orthologous proteins in 1,149 proteobacterial genomes. Our analysis reveals a significant positive correlation between protein binding frequency with DnaK and evolutionary rate. Proteins with high binding affinity to DnaK evolve on average 4.3-fold faster than proteins in the lowest binding affinity class at the genus resolution. Differences in evolutionary rates of DnaK interactor classes are still significant after adjusting for possible effects caused by protein expression level. Furthermore, we observe an additiv...Continue Reading

References

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Nov 5, 2016·Current Opinion in Structural Biology·Shimon BershteinEugene I Shakhnovich
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Datasets Mentioned

BETA
K12
MG1655

Methods Mentioned

BETA
protein folding
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Related Concepts

DnaK protein, E coli
Alkalescens-Dispar Group
Plasma Protein Binding Capacity
Genome, Bacterial
Deletion Mutation
Molecular Chaperones
GroEL Protein
Heat-Shock Proteins 70
HSP90 Heat-Shock Proteins
Evolution, Molecular

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