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Chaperone client proteins evolve slower than non-client proteins.

Manish Prakash Victor1, Debarun Acharya2, Sandip Chakraborty3

  • 1Division of Bioinformatics, Bose Institute, Kolkata, West Bengal, India.

Functional & Integrative Genomics
|May 8, 2020
PubMed
Summary

Molecular chaperones help proteins fold correctly. This study found chaperone client proteins evolve slower, suggesting chaperones protect organisms from harmful mutations by aiding protein folding.

Keywords:
ChaperoneChaperone client proteinsEvolutionary rateProtein aggregation propensityProtein folding rate

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Area of Science:

  • Molecular biology
  • Evolutionary biology
  • Protein biochemistry

Background:

  • Molecular chaperones are essential for protein folding and function.
  • Previous research suggested chaperones relax sequence constraints on client proteins, potentially allowing deleterious mutations.

Purpose of the Study:

  • To investigate the evolutionary rates of chaperone client versus non-client proteins.
  • To determine if chaperone assistance impacts protein evolution in natural conditions.

Main Methods:

  • Comparative analysis of evolutionary rates.
  • Examination of five model organisms (prokaryotic and eukaryotic).
  • Assessment of folding rates and aggregation propensity.

Main Results:

  • Chaperone client proteins exhibit significantly slower evolutionary rates across all studied organisms.
  • Client proteins demonstrate slower folding rates and reduced aggregation propensity.
  • These findings suggest chaperones mitigate the negative effects of mutations on protein folding.

Conclusions:

  • Chaperones play a crucial role in maintaining protein homeostasis by counteracting deleterious mutations.
  • The slower evolution of client proteins indicates a selective pressure against accumulating mutations that compromise protein structure/function.
  • Organisms benefit from chaperone-assisted folding, preventing the fixation of potentially harmful mutations in natural populations.