Related Experiment Video
Updated: Jun 1, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
Heat shock protein DnaK--substrate of actin-specific bacterial protease ECP32
A V Morozova1, S Yu Khaitlina, A Yu Malinin
1Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia. avmoro@gmail.com
Abstract:
It has been found that actin-specific bacterial protease ECP32 cleaves prokaryotic heat shock protein DnaK, which belongs to the family of heat shock proteins with molecular weight 70 kDa. We propose a new one-step method for DnaK purification using heat treatment. The technique yields ~1 mg of partially purified DnaK from 25 g of wet bacterial biomass. Polyclonal antibodies against DnaK were obtained. The degree of ECP32 catalyzed proteolysis of partially purified DnaK and that of DnaK in initial cell extracts was compared.
Related Concept Videos
Bacterial Protein Maturation
Other Stress Responses in Bacteria
Molecular Chaperones and Protein Folding
The...
Actin Filament Depolymerization
In F-actin, the ADF/cofilin proteins...
Introduction to Actin
Mechanical Protein Functions

