Ontology highlight
ABSTRACT:
SUBMITTER: Suh WC
PROVIDER: S-EPMC28024 | biostudies-literature | 1998 Dec
REPOSITORIES: biostudies-literature
Suh W C WC Burkholder W F WF Lu C Z CZ Zhao X X Gottesman M E ME Gross C A CA
Proceedings of the National Academy of Sciences of the United States of America 19981201 26
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, we provide evidence that DnaJ binds to at least two sites on the Escherichia coli Hsp70 family member DnaK: under the ATPase domain in a cleft between its two subdomains and at or near the pocket of su ...[more]