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Article

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

Journal of molecular microbiology and biotechnology - 1 Jan 2011

Maldonado Barbara, Buchanan Grant, Müller Matthias, Berks Ben C, Palmer Tracy

Abstract excerpt

The twin arginine protein transport (Tat) system transports folded proteins across the cytoplasmic membranes of prokaryotes and the thylakoid membranes of plant chloroplasts. In Escherichia coli, the TatB and TatC components form a multivalent receptor complex that binds Tat substrates. Here, we have used a genetic fusion approach to construct covalent TatC oligomers in order to probe the organisation of TatC. A...

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Identifiers

PMID: 21709427
DOI: 10.1159/000329076

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Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase.PMID 21709427Read ↗

The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.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 core TatABC complex of the twin-arginine translocase in Escherichia coli: TatC drives assembly whereas TatA is essential for stability.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 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 ↗

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

Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells.Semantic proximity Read ↗

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

A minimal Tat system from a gram-positive organism: a bifunctional TatA subunit participates in discrete TatAC and TatA complexes.Semantic proximity Read ↗

Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.Semantic proximity Read ↗

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