Synergism between a foldase and an unfoldase: Reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK

The role of bacterial Hsp40, DnaJ, is to co-chaperone the binding of misfolded or alternatively folded proteins to bacterial Hsp70, DnaK, which is an ATP-fuelled unfolding chaperone. In addition to its DnaK targeting activity, DnaJ has a weak thiol-reductase activity. In between the substrate-bindin...

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Auteurs principaux:	Rayees Ul Hassan Mattoo, America eFarina Henriquez Cuendet, Subbanna eSujatha, Andrija eFinka, Smriti ePriya, Sandeep Kumar Sharma, Pierre eGoloubinoff
Format:	Artigo
Langue:	Inglês
Publié:	Frontiers Media S.A. 2014-07-01
Collection:	Frontiers in Molecular Biosciences
Sujets:	Thioredoxins Aggregation Hsp70 chaperones protein disulfide isomerase DNAJ Homologues
Accès en ligne:	http://journal.frontiersin.org/Journal/10.3389/fmolb.2014.00007/full
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