Related Experiment Video
Updated: Jul 6, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
1Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, New York 10021.
Abstract:
The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding polypeptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.
Related Concept Videos
DNA Helicases
DNA Topoisomerases
Types and Mechanism of action
Topoisomerases are divided into two main types. Type I...
Homologous Recombination
Directing Proteins to the Rough Endoplasmic Reticulum
Single-Strand DNA Binding Proteins
Bacterial Protein Maturation

