Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor.

M. M. Igo, A. J. Ninfa, J. B. Stock, T. J. Silhavy

Research output: Contribution to journalArticlepeer-review

205 Scopus citations

Abstract

Signal transduction in the bacterial Omp, Che, and Ntr systems involves the phosphorylation and dephosphorylation of response regulators (OmpR, CheY and CheB, NRI) that share a homologous domain. We show that in the Omp system, the transmembrane sensor EnvZ, catalyzes both the phosphorylation of OmpR and the dephosphorylation of OmpR-P. The phosphorylation reaction proceeds by a mechanism shared with the Ntr and Che kinases, NRII, and CheA. EnvZ can phosphorylate NRI and can stimulate transcription from the glnAp2 promoter, and similarly, CheA can phosphorylate OmpR and can stimulate transcription from the ompF promoter. OmpR-P formed by either CheA or EnvZ is much more stable than CheY-P and NRI-P, but is rapidly hydrolyzed to OmpR and Pi by EnvZ in the presence of ATP, ADP, or nonhydrolyzable analogs of ATP. Because EnvZ is normally a transmembrane receptor with a periplasmic sensory domain, our results suggest that the role of EnvZ may be to control the intracellular concentration of OmpR-P in response to environmental signals.

Original languageEnglish (US)
Pages (from-to)1725-1734
Number of pages10
JournalGenes & development
Volume3
Issue number11
DOIs
StatePublished - Nov 1989

All Science Journal Classification (ASJC) codes

  • Genetics
  • Developmental Biology

Fingerprint Dive into the research topics of 'Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor.'. Together they form a unique fingerprint.

Cite this