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 twin-arginine translocation (Tat) system is essential for Rhizobium-legume symbiosis.

Molecular microbiology - 1 Jun 2003

Meloni Stefania, Rey Luis, Sidler Stephan, Imperial Juan, Ruiz-Argüeso Tomás, Palacios José M

Abstract excerpt

The Tat (twin-arginine translocation) system mediates export of periplasmic proteins in folded conformation. Proteins transported via Tat contain a characteristic twin-arginine motif in their signal peptide. Genetic determinants (tatABC genes) of the Tat system from Rhizobium leguminosarum bv. viciae were cloned and characterized, and a tatBC deletion mutant was constructed. The mutant lacked the ability for...

Read the complete abstract on PubMed

Topics

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

Share to Cytochromes c
Share to Hydrogenase
Share to Membrane Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Multigene Family

Share to Nitrogen Fixation

Share to Pisum sativum

Share to Rhizobium leguminosarum

Share to Symbiosis

Source

Identifiers

PMID: 12787349
DOI: 10.1046/j.1365-2958.2003.03510.x

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 twin-arginine translocation (Tat) system is essential for Rhizobium-legume symbiosis.PMID 12787349Read ↗

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

Characterization of the twin-arginine transport secretome in Sinorhizobium meliloti and evidence for host-dependent phenotypes.Semantic proximity Read ↗

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

The twin arginine transport system appears to be essential for viability in Sinorhizobium meliloti.Semantic proximity Read ↗

The twin-arginine translocation pathway in α-proteobacteria is functionally preserved irrespective of genomic and regulatory divergence.Semantic proximity Read ↗

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

Identification of protein secretion systems and novel secreted proteins in Rhizobium leguminosarum bv. viciae.Semantic proximity Read ↗

A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins.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 ↗

The Rhizobium leguminosarum tonB gene is required for the uptake of siderophore and haem as sources of iron.Semantic proximity Read ↗

Discovery of a haem uptake system in the soil bacterium Bradyrhizobium japonicum.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 ↗

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