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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Related Experiment Video

Updated: Sep 12, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Subtle Variations in a Client Protein Determine Bacterial Hsp90 Dependence.

Marie Corteggiani1, Amine Ali-Chaouche1, Miha Bahun2

  • 1Aix-Marseille Univ, CNRS, BIP UMR 7281, IMM, 31 Chemin Joseph Aiguier, 13402 Marseille, France.

Journal of Molecular Biology
|August 9, 2025
PubMed
Summary

Protein features like stability and degradation sensitivity determine if bacterial Hsp90 chaperone is required. This study compared TilS proteins from Shewanella oneidensis and E. coli to find Hsp90 dependence determinants.

Keywords:
Hsp90bacteriachaperoneclient specificityprotease

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Area of Science:

  • Molecular Biology
  • Protein Homeostasis
  • Bacterial Physiology

Background:

  • Heat shock protein 90 (Hsp90) is a conserved ATP-dependent chaperone essential for protein homeostasis.
  • Hsp90 stabilizes and activates numerous substrate proteins, known as clients.
  • The specific determinants dictating Hsp90 client dependence remain largely unknown.

Purpose of the Study:

  • To investigate the factors governing Hsp90 dependence using bacterial Hsp90 and its client TilS (TLocated in S.) as a model system.
  • To compare the Hsp90 dependence of TilS orthologs from Shewanella oneidensis (TilSSo) and Escherichia coli (TilSEc).
  • To identify specific protein features that confer Hsp90 dependence or independence.

Main Methods:

  • Comparative analysis of TilSSo and TilSEc for in vitro stability and in vivo degradation by proteases.
  • Assessment of Hsp90-TilS interactions using biochemical assays.
  • Construction and analysis of chimeric TilS proteins and site-directed mutagenesis.
  • Evaluation of bacterial growth under heat stress with heterologous TilS expression.

Main Results:

  • TilSEc exhibited higher stability, resistance to protease degradation without Hsp90, and no interaction with Hsp90, unlike TilSSo.
  • A specific region in TilSSo was identified as crucial for protease sensitivity and Hsp90-mediated protection.
  • Expression of TilSEc in S. oneidensis rendered Hsp90 dispensable under heat stress.
  • Conversely, expressing TilSSo in E. coli made Hsp90 essential for growth during heat stress.

Conclusions:

  • Protein-specific characteristics, including intrinsic stability and susceptibility to degradation, are key determinants of Hsp90 chaperone requirement in bacteria.
  • Hsp90 dependence is not solely dictated by the presence of the chaperone but also by client protein properties.
  • This study elucidates the molecular basis for differential Hsp90 client interactions between bacterial orthologs.