Article
Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.
Proceedings of the National Academy of Sciences of the United States of America - 22 Dec 1998
Suh W C, Burkholder W F, Lu C Z, Zhao X, Gottesman M E, Gross C A
Abstract excerpt
Chaperones of the Hsp70 family bind to unfolded or partially folded polypeptides to facilitate many cellular processes. ATP hydrolysis and substrate binding, the two key molecular activities of this chaperone, are modulated by the cochaperone DnaJ. By using both genetic and biochemical approaches...
Topics
- Adenosine Triphosphatases
- Amino Acid Substitution
- Bacterial Proteins
- Binding Sites
- Escherichia coli
- Escherichia coli Proteins
- HSP40 Heat-Shock Proteins
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- Kinetics
- Models, Molecular
- Molecular Chaperones
- Mutagenesis, Site-Directed
- Phenotype
- Protein Structure, Secondary
- Recombinant Proteins