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...
Main Authors: | , , , , , , |
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Format: | Article |
Language: | English |
Published: |
Frontiers Media S.A.
2014-07-01
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Series: | Frontiers in Molecular Biosciences |
Subjects: | |
Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmolb.2014.00007/full |