Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase.
The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel...
المؤلفون الرئيسيون: | Maldonado, B, Kneuper, H, Buchanan, G, Hatzixanthis, K, Sargent, F, Berks, B, Palmer, T |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2011
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مواد مشابهة
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Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component.
حسب: Lee, P, وآخرون
منشور في: (2006) -
Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase.
حسب: Maldonado, B, وآخرون
منشور في: (2011) -
TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli.
حسب: Orriss, G, وآخرون
منشور في: (2007) -
Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site
حسب: Kneuper, H, وآخرون
منشور في: (2012) -
Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity
حسب: May N. Taw, وآخرون
منشور في: (2022-09-01)