Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

A chaperone network controls the heat shock response in E. coli.

Eric Guisbert1, Christophe Herman, Chi Zen Lu

  • 1Department of Biochemistry and Biophysics, Microbiology and Immunology, and Stomatology, University of California, San Francisco, San Francisco, California 94143, USA.

Genes & Development
|November 17, 2004
PubMed
Summary

The GroEL/S chaperonin regulates the heat shock response in Escherichia coli by controlling sigma32 levels. This chaperone network enhances cellular protein folding detection.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Antibiotics stimulate protein transfer to persister cells.

Science (New York, N.Y.)·2026
Same author

The ω subunit stabilizes transcribing RNA polymerase to balance processivity and collision resolution.

bioRxiv : the preprint server for biology·2026
Same author

The phenotypic landscape of the model firmicute Bacillus subtilis.

bioRxiv : the preprint server for biology·2026
Same author

Predicting the protein interaction landscape of a free-living bacterium with pooled-AlphaFold3.

Molecular systems biology·2026
Same author

The phenotypic landscape of the mycobacterial cell.

bioRxiv : the preprint server for biology·2025
Same author

Transcription-replication collisions trigger high-fidelity replication reset.

Nucleic acids research·2025

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • The heat shock response is crucial for maintaining cellular protein homeostasis.
  • In Escherichia coli, sigma32 is the key transcription factor mediating this response.
  • The DnaK chaperone machine is a known regulator of sigma32 activity and levels.

Purpose of the Study:

  • To investigate the role of other major chaperones in regulating sigma32.
  • To determine if the GroEL/S chaperonin acts as a sigma32 regulator.
  • To elucidate the mechanism and implications of GroEL/S-mediated sigma32 regulation.

Main Methods:

  • In vivo studies involving overexpression and depletion of GroEL/S in E. coli.
  • Analysis of sigma32 activity and levels under varying GroEL/S conditions.

Related Experiment Videos

  • In vitro transcription assays using purified GroEL and sigma32 proteins.
  • Assessment of heat shock response under altered GroEL/S levels during stress.

    • Main Results:

    • GroEL/S was identified as a novel regulator of sigma32.
    • Increased GroEL/S levels decreased sigma32 activity in vivo, an effect reversed by a GroEL/S substrate.
    • Depletion of GroEL/S led to increased sigma32 levels and activity.
    • GroEL directly binds sigma32, inhibiting sigma32-dependent transcription in vitro.
    • Modulating GroEL/S levels impacted the heat shock response during cellular stress.

    Conclusions:

    • The GroEL/S chaperonin directly and indirectly regulates sigma32 activity and levels.
    • A chaperone network, including GroEL/S, provides a sensitive mechanism for detecting the cellular protein folding state.
    • This regulation enhances the accuracy and responsiveness of the heat shock response in E. coli.