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...
Hlavní autoři: | Maldonado, B, Kneuper, H, Buchanan, G, Hatzixanthis, K, Sargent, F, Berks, B, Palmer, T |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
2011
|
Podobné jednotky
-
Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component.
Autor: Lee, P, a další
Vydáno: (2006) -
Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase.
Autor: Maldonado, B, a další
Vydáno: (2011) -
TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli.
Autor: Orriss, G, a další
Vydáno: (2007) -
Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site
Autor: Kneuper, H, a další
Vydáno: (2012) -
Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity
Autor: May N. Taw, a další
Vydáno: (2022-09-01)