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The bacterial DnaK chaperone accelerates the evolution of its client proteins, similar to GroEL. High DnaK binding frequency correlates with faster protein evolution, impacting bacterial genome dynamics.

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Genomics

Background:

  • Proteins require molecular chaperones for proper folding into functional structures.
  • Chaperones like GroEL/GroES can buffer deleterious mutations, accelerating client protein evolution.
  • The evolutionary impact of other bacterial chaperones, such as DnaK, remains largely unexplored.

Purpose of the Study:

  • To investigate the effect of the bacterial DnaK (Hsp70) chaperone on the evolutionary rates of its client proteins.
  • To compare the evolutionary influence of DnaK with that of GroEL/GroES.
  • To understand the role of chaperone-mediated protein folding in bacterial genome evolution.

Main Methods:

  • Comparative proteome analysis of Escherichia coli against 1,808,565 orthologous proteins from 1,149 proteobacterial genomes.
  • Correlation analysis between DnaK binding frequency and protein evolutionary rates.
  • Statistical adjustments for protein expression levels and investigation of additive chaperone effects.

Main Results:

  • A significant positive correlation was found between DnaK binding frequency and protein evolutionary rate.
  • Proteins with high DnaK affinity evolve approximately 4.3-fold faster than those with low affinity.
  • DnaK and GroEL exhibit additive effects on the evolution of their common client proteins, with similar physicochemical profiles in their interactomes.

Conclusions:

  • DnaK-mediated protein folding significantly influences bacterial protein evolutionary dynamics.
  • Chaperone interactions, specifically with DnaK, have long-term manifestations on genome evolution.
  • These findings highlight the crucial role of chaperones in shaping bacterial adaptation and diversification.