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 Kasahara, M Articles by Shinagawa, H Search for Related Content PubMed PubMed Citation Articles by Kasahara, M Articles by Shinagawa, H

 Previous Article  |  Next Article 

J Bacteriol. 1991 November; 173(21): 6760-6765

research-article

Molecular analysis of the Salmonella typhimurium phoN gene, which encodes nonspecific acid phosphatase.

Department of Experimental Chemotherapy, Osaka University, Japan.

ABSTRACT

The phoN gene of Salmonella typhimurium encodes nonspecific acid phosphatase (EC 3.1.3.2), which is regulated by a two-component regulatory system consisting of the phoP and phoQ genes. We cloned the phoN region into a plasmid vector by complementation of a phoN mutant strain and determined the nucleotide sequence of the phoN gene and its flanking regions. The phoN gene could encode a 26-kDa protein, which was identified by the maxicell method as the product of phoN. Results of the enzyme assay and Southern hybridization with chromosomal DNA of Escherichia coli K-12 suggests that there is no phoN gene in E. coli. The regulatory pattern of phoN in E. coli and Southern hybridization analysis of the E. coli chromosome with the S. typhimurium phoP gene suggest that E. coli K-12 also harbors the phoP and phoQ genes.

This article has been cited by other articles:

• Lee, S.-W., Jeong, K.-S., Han, S.-W., Lee, S.-E., Phee, B.-K., Hahn, T.-R., Ronald, P. (2008). The Xanthomonas oryzae pv. oryzae PhoPQ Two-Component System Is Required for AvrXA21 Activity, hrpG Expression, and Virulence. J. Bacteriol. 190: 2183-2197 [Abstract] [Full Text]  
• Bernard, R., El Ghachi, M., Mengin-Lecreulx, D., Chippaux, M., Denizot, F. (2005). BcrC from Bacillus subtilis Acts as an Undecaprenyl Pyrophosphate Phosphatase in Bacitracin Resistance. J. Biol. Chem. 280: 28852-28857 [Abstract] [Full Text]  
• Macaskie, L. E., Bonthrone, K. M., Yong, P., Goddard, D. T. (2000). Enzymically mediated bioprecipitation of uranium by a Citrobacter sp.: a concerted role for exocellular lipopolysaccharide and associated phosphatase in biomineral formation. Microbiology 146: 1855-1867 [Abstract] [Full Text]  
• Chen, X., Ansai, T., Awano, S., Iida, T., Barik, S., Takehara, T. (1999). Isolation, Cloning, and Expression of an Acid Phosphatase Containing Phosphotyrosyl Phosphatase Activity from Prevotella intermedia. J. Bacteriol. 181: 7107-7114 [Abstract] [Full Text]  
• Hemrika, W., Renirie, R., Dekker, H. L., Barnett, P., Wever, R. (1997). From phosphatases to vanadium peroxidases: A similar architecture of the active site. Proc. Natl. Acad. Sci. USA 94: 2145-2149 [Abstract] [Full Text]  
• Waldburger, C. D., Sauer, R. T. (1996). Signal Detection by the PhoQ Sensor-Transmitter. CHARACTERIZATION OF THE SENSOR DOMAIN AND A RESPONSE-IMPAIRED MUTANT THAT IDENTIFIES LIGAND-BINDING DETERMINANTS. J. Biol. Chem. 271: 26630-26636 [Abstract] [Full Text]