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Article

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

The FEBS journal - 1 May 2005

Barrett Claire M L, Robinson Colin

Abstract excerpt

The twin-arginine translocation (Tat) system transports folded proteins across the bacterial plasma membrane. Three subunits, TatA, B and C, are known to be involved but their modes of action are poorly understood, as are the inter-subunit interactions occurring within Tat complexes. We have generated mutations in the single transmembrane (TM) spans of TatA and TatB, with the aim of generating structural...

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Source

Identifiers

PMID: 15853811
DOI: 10.1111/j.1742-4658.2005.04654.x

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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.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin-arginine translocase.PMID 15853811Read ↗

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 ↗

Salt sensitivity of minimal twin arginine translocases.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 ↗

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

Twin arginine translocation (Tat)-dependent export in the apparent absence of TatABC or TatA complexes using modified Escherichia coli TatA subunits that substitute for TatB.Semantic proximity Read ↗

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

Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli.Semantic proximity Read ↗

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

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

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