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Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone

The evolutionarily conserved DnaJ proteins are essential components of Hsp70 chaperone systems. The DnaJ homologue of Escherichia coli associates with chaperone substrates and mediates their ATP hydrolysis-dependent locking into the binding cavity of its Hsp70 partner, DnaK. To determine the substra...

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Bibliografische gegevens
Hoofdauteurs: Rüdiger, Stefan, Schneider-Mergener, Jens, Bukau, Bernd
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Oxford University Press 2001
Onderwerpen:
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC145471/
https://ncbi.nlm.nih.gov/pubmed/11230128
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/20.5.1042
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