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Article

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

Molecular microbiology - 1 Oct 2015

Cléon François, Habersetzer Johann, Alcock Felicity, Kneuper Holger, Stansfeld Phillip J, Basit Hajra, Wallace Mark I, Berks Ben C, Palmer Tracy

Abstract excerpt

The Tat protein export system translocates folded proteins across the bacterial cytoplasmic membrane and the plant thylakoid membrane. The Tat system in Escherichia coli is composed of TatA, TatB and TatC proteins. TatB and TatC form an oligomeric, multivalent receptor complex that binds Tat substrates, while multiple protomers of TatA assemble at substrate-bound TatBC receptors to facilitate substrate transport....

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Identifiers

PMID: 26112072
DOI: 10.1111/mmi.13106
PMCID: PMC5102672

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The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.PMID 26112072Read ↗

Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein 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 ↗

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

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

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

Diversity and evolution of bacterial twin arginine translocase protein, TatC, reveals a protein secretion system that is evolving to fit its environmental niche.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 ↗

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

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