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Article

The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.

The Journal of biological chemistry - 9 Jul 2010

Horne B Erin, Li Tingfeng, Genevaux Pierre, Georgopoulos Costa, Landry Samuel J

Abstract excerpt

The Escherichia coli Hsp40 DnaJ uses its J-domain (Jd) to couple ATP hydrolysis and client protein capture in Hsp70 DnaK. Fusion of the Jd to peptide p5 (as in Jdp5) dramatically increases the apparent affinity of the p5 moiety for DnaK in the presence of ATP, and Jdp5 stimulates ATP hydrolysis in DnaK by several orders of magnitude. NMR experiments with [(15)N]Jdp5 demonstrated that the peptide tethers the Jd to...

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Identifiers

PMID: 20448033
DOI: 10.1074/jbc.M110.113118
PMCID: PMC2898438

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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