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The Hsp40 J-domain Stimulates Hsp70 When Tethered by the Client to the ATPase Domain
The Escherichia coli Hsp40 DnaJ uses its J-domain (Jd) to couple ATP hydrolysis and client protein capture in Hsp70 DnaK. Fusion of the Jd to peptide p5 (as in Jdp5) dramatically increases the apparent affinity of the p5 moiety for DnaK in the presence of ATP, and Jdp5 stimulates ATP hydrolysis in D...
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| Asıl Yazarlar: | , , , , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
American Society for Biochemistry and Molecular Biology
2010
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2898438/ https://ncbi.nlm.nih.gov/pubmed/20448033 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.113118 |
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