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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Detalles Bibliográficos
Publicado en:Front Mol Biosci
Main Authors: Mattoo, Rayees U. H., Farina Henriquez Cuendet, America, Subanna, Sujatha, Finka, Andrija, Priya, Smriti, Sharma, Sandeep K., Goloubinoff, Pierre
Formato: Artigo
Idioma:Inglês
Publicado: Frontiers Media S.A. 2014
Assuntos:
Molecular Biosciences
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC4428491/
https://ncbi.nlm.nih.gov/pubmed/25988148
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3389/fmolb.2014.00007
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