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Article

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

Scientific reports - 14 Jun 2024

Werner Max-Hinrich, Mehner-Breitfeld Denise, Brüser Thomas

Abstract excerpt

The twin-arginine translocation (Tat) system transports folded proteins across energized biological membranes in bacteria, plastids, and plant mitochondria. In Escherichia coli, the three membrane proteins TatA, TatB and TatC associate to enable Tat transport. While TatB and TatC together form complexes that bind Tat-dependently transported proteins, the TatA component is responsible for the permeabilization of...

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Identifiers

PMID: 38877109
DOI: 10.1038/s41598-024-64547-x
PMCID: PMC11178869

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

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A larger TatBC complex associates with TatA clusters for transport of folded proteins across the bacterial cytoplasmic membrane.PMID 38877109Read ↗

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 ↗

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

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

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 ↗

A mutation leading to super-assembly of twin-arginine translocase (Tat) protein complexes.Semantic proximity Read ↗

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