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Article

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.

Proceedings of the National Academy of Sciences of the United States of America - 11 May 1999

Laufen T, Mayer M P, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B

Abstract excerpt

Hsp70 chaperones assist a large variety of protein folding processes within the entire lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ cochaperones. DnaJ stimulates Hsp70 to hydrolyze ATP, a key step that closes its substrate-binding cavity and thus allows stable binding of substrate. We show that DnaJ stimulates ATP hydrolysis by Escherichia coli Hsp70, DnaK, very efficiently...

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Identifiers

PMID: 10318904
DOI: 10.1073/pnas.96.10.5452
PMCID: PMC21880

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones.PMID 10318904Read ↗

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