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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 7 Mar 2017

Huang Qi, Alcock Felicity, Kneuper Holger, Deme Justin C, Rollauer Sarah E, Lea Susan M, Berks Ben C, Palmer Tracy

Abstract excerpt

The twin-arginine protein translocation (Tat) system mediates transport of folded proteins across the cytoplasmic membrane of bacteria and the thylakoid membrane of chloroplasts. The Tat system of Escherichia coli is made up of TatA, TatB, and TatC components. TatBC comprise the substrate receptor complex, and active Tat translocases are formed by the substrate-induced association of TatA oligomers with this...

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Identifiers

PMID: 28223511
DOI: 10.1073/pnas.1615056114
PMCID: PMC5347605

Provenance

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→

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A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.PMID 28223511Read ↗

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

Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides.Semantic proximity Read ↗

Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins.Semantic proximity Read ↗

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

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

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 ↗

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 ↗

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 ↗

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

Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone.Semantic proximity Read ↗

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