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Article

Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation.

Journal of bacteriology - 1 Nov 2002

Lee Philip A, Buchanan Grant, Stanley Nicola R, Berks Ben C, Palmer Tracy

Abstract excerpt

The TatA and TatB proteins are essential components of the twin arginine protein translocation pathway in Escherichia coli. C-terminal truncation analysis of the TatA protein revealed that a plasmid-expressed TatA protein shortened by 40 amino acids is still fully competent to support protein tra...

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Identifiers

PMID: 12374820
DOI: 10.1128/JB.184.21.5871-5879.2002
PMCID: PMC135397

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12374820-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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Truncation analysis of TatA and TatB defines the minimal functional units required for protein translocation.PMID 12374820Read ↗

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

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 ↗

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 ↗

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

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

Two minimal Tat translocases in Bacillus.Semantic proximity Read ↗

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

Salt sensitivity of minimal twin arginine translocases.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 ↗

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