This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Waukau, J Articles by Forst, S Search for Related Content PubMed PubMed Citation Articles by Waukau, J Articles by Forst, S

 Previous Article  |  Next Article 

J Bacteriol. 1992 March; 174(5): 1522-1527

research-article

Molecular analysis of the signaling pathway between EnvZ and OmpR in Escherichia coli.

J Waukau and S Forst

Department of Biological Sciences, University of Wisconsin-Milwaukee 53201.

ABSTRACT

OmpR is a DNA-binding protein that regulates transcription of ompF and ompC. The activity of OmpR is controlled by the inner membrane osmosensor, EnvZ. In order to study the signaling process between EnvZ and OmpR, we analyzed two different envZ strains: the envZ473 strain, in which OmpC is constitutively produced and OmpF is fully repressed, and the envZ3 strain, in which the production of OmpC is greatly reduced and OmpF is not fully repressed by high-osmolarity growth conditions. Using direct sequencing of DNA derived from the polymerase chain reaction amplification method, we identified the mutation in the envZ473 strain as a Val-241-to-Gly substitution and the mutation in the envZ3 as an Ala-219-to-Val substitution. The relative DNA-binding affinity of OmpR derived from the envZ473 strain was dramatically increased for the upstream sequence of both ompF and ompC. In contrast, OmpR derived from the envZ3 strain was not converted to the high-affinity form. The intracellular levels of OmpR-phosphate, as analyzed by the in vivo phosphorylation approach, significantly increased in the envZ473 strain, while in the envZ3 strain the levels were considerably reduced, relative to those found in the parent strain. The intracellular level of OmpR protein in the envZ473 strain was also found to be markedly elevated relative to that of the parent strain. These results are discussed in relation to the role of phosphorylation and relative DNA-binding affinity of OmpR in the expression of ompF and ompC.

---

J Bacteriol. 1992 March; 174(5): 1522-1527

This article has been cited by other articles:

• Anjum, S., Doucet, A., Holmes, C. C. (2009). A boosting approach to structure learning of graphs with and without prior knowledge. Bioinformatics 25: 2929-2936 [Abstract] [Full Text]  
• Kishii, R., Falzon, L., Yoshida, T., Kobayashi, H., Inouye, M. (2007). Structural and Functional Studies of the HAMP Domain of EnvZ, an Osmosensing Transmembrane Histidine Kinase in Escherichia coli. J. Biol. Chem. 282: 26401-26408 [Abstract] [Full Text]  
• Zhu, Y., Inouye, M. (2004). The HAMP Linker in Histidine Kinase Dimeric Receptors Is Critical for Symmetric Transmembrane Signal Transduction. J. Biol. Chem. 279: 48152-48158 [Abstract] [Full Text]  
• Zhu, Y., Inouye, M. (2003). Analysis of the Role of the EnvZ Linker Region in Signal Transduction Using a Chimeric Tar/EnvZ Receptor Protein, Tez1. J. Biol. Chem. 278: 22812-22819 [Abstract] [Full Text]  
• Waukau, J., Forst, S. (1999). Identification of a Conserved N-Terminal Sequence Involved in Transmembrane Signal Transduction in EnvZ. J. Bacteriol. 181: 5534-5538 [Abstract] [Full Text]  
• Berlyn, M. K. B. (1998). Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map. Microbiol. Mol. Biol. Rev. 62: 814-984 [Abstract] [Full Text]  
• Barrett, J. F., Hoch, J. A. (1998). Two-Component Signal Transduction as a Target for Microbial Anti-Infective Therapy. Antimicrob. Agents Chemother. 42: 1529-1536 [Full Text]  
• Boos, W., Shuman, H. (1998). Maltose/Maltodextrin System of Escherichia coli: Transport, Metabolism, and Regulation. Microbiol. Mol. Biol. Rev. 62: 204-229 [Abstract] [Full Text]