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The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.
The chaperone SecB keeps precursor proteins in a translocation-competent state and targets them to SecA at the translocation sites in the cytoplasmic membrane of Escherichia coli. SecA is thought to recognize SecB via its carboxy-terminus. To determine the minimal requirement for a SecB-binding site...
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| Autori principali: | , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
1997
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1326294/ https://ncbi.nlm.nih.gov/pubmed/9321390 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/16.20.6105 |
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