Recent advances in understanding catalysis of protein folding by molecular chaperones

FEBS Lett. 2020 Sep;594(17):2770-2781. doi: 10.1002/1873-3468.13844. Epub 2020 Jun 12.

Abstract

Molecular chaperones are highly conserved proteins that promote proper folding of other proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking, the assembly of oligomeric complexes, and recovery from stress-induced unfolding. A fundamental function of molecular chaperones is to inhibit unproductive protein interactions by recognizing and protecting hydrophobic surfaces that are exposed during folding or following proteotoxic stress. Beyond this basic principle, it is now clear that chaperones can also actively and specifically accelerate folding reactions in an ATP-dependent manner. We focus on the bacterial Hsp70 and chaperonin systems as paradigms, and review recent work that has advanced our understanding of how these chaperones act as catalysts of protein folding.

Keywords: DnaK; GroEL; Hsp40; Hsp60; Hsp70; chaperonin; confinement; molecular chaperones; protein folding; protein misfolding.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphate / chemistry*
  • Adenosine Triphosphate / metabolism
  • Biocatalysis
  • Chaperonin 60 / chemistry*
  • Chaperonin 60 / genetics
  • Chaperonin 60 / metabolism
  • Chaperonins / chemistry*
  • Chaperonins / genetics
  • Chaperonins / metabolism
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Gene Expression Regulation, Bacterial
  • HSP70 Heat-Shock Proteins / chemistry*
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / metabolism
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Folding
  • Protein Interaction Domains and Motifs
  • Protein Unfolding

Substances

  • Chaperonin 60
  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • Molecular Chaperones
  • Adenosine Triphosphate
  • Chaperonins
  • dnaK protein, E coli