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Article

Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase.

FEBS letters - 4 Feb 2011

Maldonado Barbara, Kneuper Holger, Buchanan Grant, Hatzixanthis Kostas, Sargent Frank, Berks Ben C, Palmer Tracy

Abstract excerpt

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 contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex...

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Identifiers

PMID: 21237157
DOI: 10.1016/j.febslet.2011.01.016

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase.PMID 21237157Read ↗

Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin-arginine translocase.Semantic proximity Read ↗

Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation.Semantic proximity Read ↗

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Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase.Semantic proximity Read ↗

Escherichia coli twin arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities.Semantic proximity Read ↗

The entire N-terminal half of TatC is involved in twin-arginine precursor binding.Semantic proximity Read ↗

The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Semantic proximity Read ↗

Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component.Semantic proximity Read ↗

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