Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation
SecA, a 102-kDa hydrophilic protein, couples the energy of ATP binding to the translocation of preprotein across the bacterial inner membrane. SecA function and topology were studied with metabolically labeled [(35)S]SecA and with inner membrane vesicles from cells that overexpressed SecYEGDFyajC, t...
Sparad:
| I publikationen: | Proc Natl Acad Sci U S A |
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| Huvudupphov: | , |
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Utgiven: |
National Academy of Sciences
1997
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC20820/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9159114/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.94.11.5574 |
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