Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo.
Chaperone proteins bind to newly synthesized polypeptides and assist in various assembly reactions. The Escherichia coli chaperone protein SecB binds precursors of exported proteins and assists in export. In vitro, SecB can bind to many unfolded proteins. In this report, we demonstrate that SecB bin...
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| Yayımlandı: | J Bacteriol |
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| Asıl Yazarlar: | , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
American Society for Microbiology (ASM)
1993
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC204502/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8468278/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.175.8.2184-2188.1993 |
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