Export of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutations.
It is believed that one or more basic residues at the extreme amino terminus of precursor proteins and the lack of a net positive charge immediately following the signal peptide act as topological determinants that promote the insertion of the signal peptide hydrophobic core into the cytoplasmic mem...
Guardado en:
| Publicado en: | J Bacteriol |
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| Autores principales: | , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Microbiology (ASM)
1992
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC205681/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1729228/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.174.1.92-101.1992 |
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