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Article

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

The Journal of biological chemistry - 10 Nov 2006

Lee Philip A, Orriss George L, Buchanan Grant, Greene Nicholas P, Bond Peter J, Punginelli Claire, Jack Rachael L, Sansom Mark S P, Berks Ben C, Palmer Tracy

Abstract excerpt

The cytoplasmic membrane protein TatB is an essential component of the Escherichia coli twin-arginine (Tat) protein translocation pathway. Together with the TatC component it forms a complex that functions as a membrane receptor for substrate proteins. Structural predictions suggest that TatB is anchored to the membrane via an N-terminal transmembrane alpha-helix that precedes an amphipathic alpha-helical section...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16973610
DOI: 10.1074/jbc.M607295200

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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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Cysteine-scanning mutagenesis and disulfide mapping studies of the conserved domain of the twin-arginine translocase TatB component.PMID 16973610Read ↗

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

A larger TatBC complex associates with TatA clusters for transport of folded proteins across the bacterial cytoplasmic membrane.Semantic proximity Read ↗

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

Mutations in subunits of the Escherichia coli twin-arginine translocase block function via differing effects on translocation activity or tat complex structure.Semantic proximity Read ↗

The core TatABC complex of the twin-arginine translocase in Escherichia coli: TatC drives assembly whereas TatA is essential for stability.Semantic proximity Read ↗

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

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

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

A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.Semantic proximity Read ↗

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

Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein.Semantic proximity Read ↗

Salt sensitivity of minimal twin arginine translocases.Semantic proximity Read ↗

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