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Article

The linker region plays an important role in the interdomain communication of the response regulator OmpR.

The Journal of biological chemistry - 6 Sept 2002

Mattison Kirsten, Oropeza Ricardo, Kenney Linda J

Abstract excerpt

OmpR is the response regulator of a two-component regulatory system that controls the expression of the porin genes ompF and ompC in Escherichia coli. This regulator consists of two domains joined by a flexible linker region. The amino-terminal domain is phosphorylated by the sensor kinase EnvZ, and the carboxyl-terminal domain binds DNA via a winged helix-turn-helix motif. In vitro studies have shown that...

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PMID: 12077136
DOI: 10.1074/jbc.M204122200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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The linker region plays an important role in the interdomain communication of the response regulator OmpR.PMID 12077136Read ↗

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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. Phosphorylation-independent mechanism of activation by an OmpR mutant.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 ↗

The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor.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 ↗

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