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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| Pubblicato in: | EMBO J |
|---|---|
| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Nature Publishing Group
2001
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC145471/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11230128/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/20.5.1042 |
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