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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...

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Detaylı Bibliyografya
Yayımlandı:Proc Natl Acad Sci U S A
Asıl Yazarlar: Eichler, Jerry, Wickner, William
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: National Academy of Sciences 1997
Konular:
Online Erişim: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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