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

The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules.

The EMBO journal - 6 Aug 2008

Matos Cristina F R O, Robinson Colin, Di Cola Alessandra

Abstract excerpt

The twin-arginine translocation (Tat) system transports folded proteins across the bacterial plasma membrane, including FeS proteins that receive their cofactors in the cytoplasm. We have studied two Escherichia coli Tat substrates, NrfC and NapG, to examine how, or whether, the system exports only correctly folded and assembled FeS proteins. With NrfC, substitutions in even one of four predicted FeS centres...

Read the complete abstract on PubMed

Topics

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

Share to Carboxylic Ester Hydrolases
Share to Iron-Sulfur Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Transport Proteins

Share to Oxidoreductases

Share to Protein Folding

Share to Protein Sorting Signals

Share to Protein Subunits

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 18615097
DOI: 10.1038/emboj.2008.132
PMCID: PMC2516881

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Tat system proofreads FeS protein substrates and directly initiates the disposal of rejected molecules.PMID 18615097Read ↗

Proofreading of substrate structure by the Twin-Arginine Translocase is highly dependent on substrate conformational flexibility but surprisingly tolerant of surface charge and hydrophobicity changes.Semantic proximity Read ↗

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

Functional Tat transport of unstructured, small, hydrophilic proteins.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 ↗

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

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

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

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

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

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

Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway.Semantic proximity Read ↗

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