A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.

The Escherichia coli heat-shock protein DnaJ cooperates with the Hsp70 homolog DnaK in protein folding in vitro and in vivo. Little is known about the structural features of DnaJ that mediate its interaction with DnaK and unfolded polypeptide. DnaJ contains at least four blocks of sequence represent...

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Bibliographic Details
Published in:EMBO J
Main Authors: Szabo, A, Korszun, R, Hartl, F U, Flanagan, J
Format: Artigo
Language:Inglês
Published: Nature Publishing Group 1996
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Research Article
Online Access:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC449956/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8617216/
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