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

Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor.

Genes & development - 15 Sept 2004

Kato Akinori, Groisman Eduardo A

Abstract excerpt

A fundamental question in signal transduction is how an organism integrates multiple signals into a cellular response. Here we report the mechanism by which the Salmonella PmrA/PmrB two-component system responds to the signal controlling the PhoP/PhoQ two-component system. We establish that the PhoP-activated PmrD protein binds to the phosphorylated form of the response regulator PmrA, preventing both its...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Gene Expression Regulation, Bacterial

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

Share to Magnesium

Share to Phosphorylation

Share to Protein Processing, Post-Translational

Share to Protein Structure, Tertiary

Share to Salmonella enterica

Share to Transcription, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 15371344
DOI: 10.1101/gad.1230804
PMCID: PMC517523

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

Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensor.PMID 15371344Read ↗

Closing the loop: the PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD.Semantic proximity Read ↗

A small protein that mediates the activation of a two-component system by another two-component system.Semantic proximity Read ↗

Acetyl phosphate-dependent activation of a mutant PhoP response regulator that functions independently of its cognate sensor kinase.Semantic proximity Read ↗

Genetic evidence for a periplasmic protein as a component for a subset of NtrYX two-component systemsSemantic proximity Read ↗

Two-Component Regulatory Systems of MycobacteriaSemantic proximity Read ↗

PmrD is required for modifications to escherichia coli endotoxin that promote antimicrobial resistance.Semantic proximity Read ↗

A comparative proteomic analysis of Salmonella typhimurium under the regulation of the RstA/RstB and PhoP/PhoQ systems.Semantic proximity Read ↗

Structural insights into the signal transduction mechanism of the K+-sensing two-component system KdpDE.Semantic proximity Read ↗

Phosphorylated CpxR restricts production of the RovA global regulator in Yersinia pseudotuberculosis.Semantic proximity Read ↗

Listeria monocytogenes Requires the RsbX Protein To Prevent SigB Activation under Nonstressed Conditions.Semantic proximity Read ↗

Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon.Semantic proximity Read ↗

A two-component phosphotransfer network involving ArcB, ArcA, and RssB coordinates synthesis and proteolysis of sigmaS (RpoS) in E. coli.Semantic proximity Read ↗

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