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

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

The Journal of biological chemistry - 16 Mar 2007

Kreutzenbeck Peter, Kröger Carsten, Lausberg Frank, Blaudeck Natascha, Sprenger Georg A, Freudl Roland

Abstract excerpt

The twin arginine (Tat) secretion pathway allows the translocation of folded proteins across the cytoplasmic membrane of bacteria. Tat-specific signal peptides contain a characteristic amino acid motif ((S/T)RRXFLK) including two highly conserved consecutive arginine residues that are thought to be involved in the recognition of the signal peptides by the Tat translocase. Here, we have analyzed the specificity of...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Glutamine

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

Share to Lysine

Share to Membrane Transport Proteins

Share to Mutagenesis

Share to Protein Sorting Signals

Share to Protein Transport

Share to Signal Recognition Particle

Source

Identifiers

PMID: 17229735
DOI: 10.1074/jbc.M610126200

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

Escherichia coli twin arginine (Tat) mutant translocases possessing relaxed signal peptide recognition specificities.PMID 17229735Read ↗

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 ↗

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

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

Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides.Semantic proximity Read ↗

Salt sensitivity of minimal twin arginine translocases.Semantic proximity Read ↗

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

Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins.Semantic proximity Read ↗

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

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

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

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