Heat-inactivated proteins are rescued by the DnaK⋅J-GrpE set and ClpB chaperones
Functional chaperone cooperation between Hsp70 (DnaK) and Hsp104 (ClpB) was demonstrated in vitro. In a eubacterium Thermus thermophilus, DnaK and DnaJ exist as a stable trigonal ring complex (TDnaK⋅J complex) and the dnaK gene cluster contains a clpB gene. When substrate proteins were heated at hig...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1999
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC22047/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10377389/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.13.7184 |
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