Article
The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein.
The Journal of biological chemistry - 5 Aug 1991
Liberek K, Skowyra D, Zylicz M, Johnson C, Georgopoulos C
Abstract excerpt
The DnaK protein of Escherichia coli and its eukaryotic hsp70 analogues are known to bind some polypeptides and to release or dissociate from them following ATP hydrolysis. Here we demonstrate that hydrolysis (and not simply binding) of nucleotide triphosphates leads to a change in the DnaK prote...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Bacterial Proteins
- Cytidine Triphosphate
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Escherichia coli Proteins
- Guanosine Triphosphate
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- Hydrolysis
- Mutation
- Protein Conformation