Hsp90, a team player in protein quality control and the stress response in bacteria

Microbiol Mol Biol Rev. 2024 Jun 27;88(2):e0017622. doi: 10.1128/mmbr.00176-22. Epub 2024 Mar 27.

Abstract

SUMMARYHeat shock protein 90 (Hsp90) participates in proteostasis by facilitating protein folding, activation, disaggregation, prevention of aggregation, degradation, and protection against degradation of various cellular proteins. It is highly conserved from bacteria to humans. In bacteria, protein remodeling by Hsp90 involves collaboration with the Hsp70 molecular chaperone and Hsp70 cochaperones. In eukaryotes, protein folding by Hsp90 is more complex and involves collaboration with many Hsp90 cochaperones as well as Hsp70 and Hsp70 cochaperones. This review focuses primarily on bacterial Hsp90 and highlights similarities and differences between bacterial and eukaryotic Hsp90. Seminal research findings that elucidate the structure and the mechanisms of protein folding, disaggregation, and reactivation promoted by Hsp90 are discussed. Understanding the mechanisms of bacterial Hsp90 will provide fundamental insight into the more complex eukaryotic chaperone systems.

Keywords: DnaJ; DnaK; Hsp40; Hsp70; Hsp90; HtpG; client; cochaperone.

Publication types

  • Review

MeSH terms

  • Bacteria* / metabolism
  • Bacterial Proteins* / metabolism
  • HSP70 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins* / metabolism
  • Humans
  • Molecular Chaperones / metabolism
  • Protein Folding*
  • Proteostasis / physiology
  • Stress, Physiological

Substances

  • HSP90 Heat-Shock Proteins
  • Bacterial Proteins
  • HSP70 Heat-Shock Proteins
  • Molecular Chaperones