Both linked and unlinked mutations can alter the intracellular site of synthesis of exported proteins of Escherichia coli.
It previously has been demonstrated that synthesis of the periplasmic maltose-binding protein (MBP) and alkaline phosphatase (AP) of Eschericha coli predominantly occurs on membrane-bound polysomes. In this study, signal sequence alterations that adversely affect export of MBP and AP, resulting in t...
Uloženo v:
| Vydáno v: | J Bacteriol |
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| Hlavní autoři: | , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
1985
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC214865/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3881389/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.161.1.258-264.1985 |
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