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

A single amino acid substitution in the C terminus of OmpR alters DNA recognition and phosphorylation.

Journal of molecular biology - 23 Jun 2000

Tran V K, Oropeza R, Kenney L J

Abstract excerpt

In bacteria and lower eukaryotes, adaptation to changes in the environment is often mediated by two-component regulatory systems. Such systems provide the basis for chemotaxis, nitrogen and phosphate regulation and adaptation to osmotic stress, for example. In Escherichia coli, the sensor kinase EnvZ detects a change in the osmotic environment and phosphorylates the response regulator OmpR. Phospho-OmpR binds to...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Outer Membrane Proteins
Share to beta-Galactosidase
Share to Molecular Weight

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

Share to Multienzyme Complexes

Share to Phosphates

Share to Porins

Share to Response Elements

Share to Thermodynamics

Source

Identifiers

PMID: 10873450
DOI: 10.1006/jmbi.2000.3809

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

A single amino acid substitution in the C terminus of OmpR alters DNA recognition and phosphorylation.PMID 10873450Read ↗

A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC.Semantic proximity Read ↗

Gene activation by the Escherichia coli positive regulator, OmpR. Phosphorylation-independent mechanism of activation by an OmpR mutant.Semantic proximity Read ↗

Relative binding affinities of OmpR and OmpR-phosphate at the ompF and ompC regulatory sites.Semantic proximity Read ↗

Signal transduction and osmoregulation in Escherichia coli. A novel type of mutation in the phosphorylation domain of the activator protein, OmpR, results in a defect in its phosphorylation-dependent DNA binding.Semantic proximity Read ↗

Molecular analysis of the signaling pathway between EnvZ and OmpR in Escherichia coli.Semantic proximity Read ↗

Intramolecular second-site revertants to the phosphorylation site mutation in OmpR, a kinase-dependent transcriptional activator in Escherichia coli.Semantic proximity Read ↗

Amino acids important for DNA recognition by the response regulator OmpR.Semantic proximity Read ↗

Signal transduction and osmoregulation in Escherichia coli: a novel mutant of the positive regulator, OmpR, that functions in a phosphorylation-independent manner.Semantic proximity Read ↗

Mutations in a central highly conserved non-DNA-binding region of OmpR, an Escherichia coli transcriptional activator, influence its DNA-binding ability.Semantic proximity Read ↗

Gene activation by the Escherichia coli positive regulator OmpR: a mutational study of the DNA-binding domain of OmpR.Semantic proximity Read ↗

Molecular basis for promoter selectivity of the transcriptional activator OmpR of Escherichia coli: isolation of mutants that can activate the non-cognate kdpABC promoter.Semantic proximity Read ↗

A novel sensor-regulator protein that belongs to the homologous family of signal-transduction proteins involved in adaptive responses in Escherichia coli.Semantic proximity Read ↗

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