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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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| Publicado no: | Front Mol Biosci |
|---|---|
| Main Authors: | , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Frontiers Media S.A.
2014
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| Assuntos: | |
| Acesso em linha: | 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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