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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, we provide evidence that DnaJ binds to at least two sites on the Escherichia coli Hsp70 family member DnaK: under the...

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Identifiers

PMID: 9860950
DOI: 10.1073/pnas.95.26.15223
PMCID: PMC28024

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Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.PMID 9860950Read ↗

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