Related Experiment Video
Updated: Jun 18, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
Published on: October 23, 2016
Prevention of protein denaturation under heat stress by the chaperonin Hsp60
J Martin1, A L Horwich, F U Hartl
1Program of Cellular Biochemistry and Biophysics, Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, NY 10021.
Abstract:
The increased synthesis of heat shock proteins is a ubiquitous physiological response of cells to environmental stress. How these proteins function in protecting cellular structures is not yet understood. The mitochondrial heat shock protein 60 (Hsp60) has now been shown to form complexes with a variety of polypeptides in organelles exposed to heat stress. The Hsp60 was required to prevent the thermal inactivation in vivo of native dihydrofolate reductase (DHFR) imported into mitochondria. In vitro, Hsp60 bound to DHFR in the course of thermal denaturation, preventing its aggregation, and mediated its adenosine triphosphate-dependent refolding at increased temperatures. These results suggest a general mechanism by which heat shock proteins of the Hsp60 family stabilize preexisting proteins under stress conditions.
More Related Videos
10:24Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
07:14Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
Related Concept Videos
Protein Folding
Molecular Chaperones and Protein Folding
The...
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Molecular Chaperones and Protein Folding
The...
Protein Denaturation
Bacterial Protein Maturation