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Article

Role of DnaJ G/F-rich domain in conformational recognition and binding of protein substrates.

The Journal of biological chemistry - 29 Oct 2010

Perales-Calvo Judit, Muga Arturo, Moro Fernando

Abstract excerpt

DnaJ from Escherichia coli is a Type I Hsp40 that functions as a cochaperone of DnaK (Hsp70), stimulating its ATPase activity and delivering protein substrates. How DnaJ binds protein substrates is still poorly understood. Here we have studied the role of DnaJ G/F-rich domain in binding of several substrates with different conformational properties (folded, partially (un)folded and unfolded). Using partial...

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Identifiers

PMID: 20729526
DOI: 10.1074/jbc.M110.144642
PMCID: PMC2962521

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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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