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Molecular Chaperones and Protein Folding

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Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...

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Updated: Jun 24, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70

Published on: March 8, 2024

Sequential interplay between BAG6 and HSP70 upon heat shock.

A Corduan¹, S Lecomte, C Martin

¹Université de Rennes1, Interactions Cellulaires et Moléculaires UMR6026 CNRS-Hip-IFR140 GFAS, Bâtiment 13, Campus de Beaulieu, 35042, Rennes cedex, France.

Cellular and Molecular Life Sciences : CMLS

|April 10, 2009

Summary

This summary is machine-generated.

Heat shock protein HSP70 accumulation requires BAG6. Subsequently, HSP70 triggers BAG6 degradation via the ubiquitin-proteasome system, regulating cellular protein homeostasis.

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Last Updated: Jun 24, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70

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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

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Intracellular Refolding Assay

Intracellular Refolding Assay

Published on: January 24, 2012

Area of Science:

Molecular Biology
Cellular Stress Response

Background:

BAG6 (also known as Scythe/Bat3) is a cochaperone of heat shock protein 70 (HSP70).
BAG6 influences HSP70's protein-refolding activity, but its role in proteotoxic stress is unclear.

Purpose of the Study:

To elucidate the precise role of BAG6 in cellular responses to proteotoxic stress, specifically its interaction with HSP70.

Main Methods:

Investigated the accumulation of HSP70 upon heat shock.
Analyzed the degradation of BAG6 in response to HSP70 accumulation.
Utilized ubiquitin-proteasome system assays.

Main Results:

BAG6 is essential for HSP70 accumulation during heat shock.
Accumulated HSP70 induces rapid, CHIP-independent degradation of BAG6 via the ubiquitin-proteasome system.
Demonstrated reciprocal regulation between BAG6 and HSP70.

Conclusions:

BAG6 acts as a central regulator of cellular HSP70 levels.
HSP70-mediated degradation of BAG6 may facilitate HSP70's refolding activity and control its induction levels.