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

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...

Full description

Bibliographic Details
Main Authors: Rayees Ul Hassan Mattoo, America eFarina Henriquez Cuendet, Subbanna eSujatha, Andrija eFinka, Smriti ePriya, Sandeep Kumar Sharma, Pierre eGoloubinoff
Format: Article
Language:English
Published: Frontiers Media S.A. 2014-07-01
Series:Frontiers in Molecular Biosciences
Subjects:
Thioredoxins
Aggregation
Hsp70
chaperones
protein disulfide isomerase
DNAJ Homologues
Online Access:http://journal.frontiersin.org/Journal/10.3389/fmolb.2014.00007/full

Internet

http://journal.frontiersin.org/Journal/10.3389/fmolb.2014.00007/full

Similar Items