Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli.

PloS one - 1 Jan 2012

Lausberg Frank, Fleckenstein Stefan, Kreutzenbeck Peter, Fröbel Julia, Rose Patrick, Müller Matthias, Freudl Roland

Abstract excerpt

The twin arginine translocation (Tat) pathway transports folded proteins across the cytoplasmic membrane of bacteria. Tat signal peptides contain a consensus motif (S/T-R-R-X-F-L-K) that is thought to play a crucial role in substrate recognition by the Tat translocase. Replacement of the phenylalanine at the +2 consensus position in the signal peptide of a Tat-specific reporter protein (TorA-MalE) by aspartate...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Escherichia coli
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Membrane Transport Proteins

Share to Mutation

Share to Phenylalanine

Share to Protein Sorting Signals

Source

Open in PubMed Open full text

Identifiers

PMID: 22761916
DOI: 10.1371/journal.pone.0039867
PMCID: PMC3383694

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Genetic evidence for a tight cooperation of TatB and TatC during productive recognition of twin-arginine (Tat) signal peptides in Escherichia coli.PMID 22761916Read ↗

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 ↗

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

Competition between Sec- and TAT-dependent protein translocation in Escherichia coli.Semantic proximity Read ↗

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

Mapping the twin-arginine protein translocation network of Bacillus subtilis.Semantic proximity Read ↗

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

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

Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane.Semantic proximity Read ↗

Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides.Semantic proximity Read ↗

In vivo dissection of the Tat translocation pathway in Escherichia coli.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.