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Protein folding in the periplasm in the absence of primary oxidant DsbA: modulation of redox potential in periplasmic space via OmpL porin
Disulfide bond formation in Escherichia coli is a catalyzed reaction accomplished by DsbA. We found that null mutations in a new porin gene, ompL, allowed a total bypass of the DsbA requirement for protein oxidation. These mutations acted as extragenic null suppressors for dsbA, and restored normal...
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| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Oxford University Press
2000
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| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC305838/ https://ncbi.nlm.nih.gov/pubmed/11080145 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/19.22.5980 |
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