The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor.
Open accessAbstract
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.
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Cites
GROWTH FACTOR RECEPTOR TYROSINE KINASES
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Protein phosphorylation and regulation of adaptive responses in bacteria
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Self-citationPhysiological and genetic responses of bacteria to osmotic stress
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Self-citationPhosphorylation of three proteins in the signaling pathway of bacterial chemotaxis
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Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
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Signal transduction schemes of bacteria
Parkinson, J. S. (1993) · Cell · doi:10.1016/0092-8674(93)90267-t · Cited by 772
Inter-kingdom signalling: Communication between bacteria and their hosts
Hughes, D. T., & Sperandio, V. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1836 · Cited by 761
Molecular Mechanisms of Two-Component Signal Transduction
Zschiedrich, C. P., Keidel, V., & Szurmant, H. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.003 · Cited by 540
Skerker, J. M., Prasol, M. S., Perchuk, B. S., Biondi, E. G., & Laub, M. T. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030334 · Cited by 435
The Histidine Protein Kinase Superfamily
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Metadata
- Authors
- Igo, M. M., Ninfa, A. J., Stock, J. B., & Silhavy, T. J.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1989-11
- Volume
- 3
- Issue
- 11
- Pages
- 1725-1734
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W1991038330
- Cited by
- 277
- References
- 35
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Igo, M. M., Ninfa, A. J., Stock, J. B., & Silhavy, T. J. (1989). Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes & Development. https://doi.org/10.1101/gad.3.11.1725
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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