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

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2005, p. 5242-5248, Vol. 187, No. 15
0021-9193/05/$08.00+0     doi:10.1128/JB.187.15.5242-5248.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of a Multigene-Encoded Sodium/Hydrogen Antiporter (Sha) from Pseudomonas aeruginosa: Its Involvement in Pathogenesis

Saori Kosono,1* Koki Haga,1 Rui Tomizawa,1 Yusuke Kajiyama,1 Kazuo Hatano,2 Shinobu Takeda,2 Yoshimi Wakai,2 Motohiro Hino,3 and Toshiaki Kudo1,4

Environmental Molecular Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan,1 Pharmacology Research Laboratories, Astellas Pharma Inc., 2-chome, 1-6, Kashima, Yodogawa-ku, Osaka 532-8514, Japan,2 Fermentation and Biotechnology Laboratories, Astellas Pharma Inc., 156 Nakagawara, Shinkawa-cho, Nishikasugai-gun, Aichi 452-0915, Japan,3 Graduate School of Integrated Science, Yokohama City University, Tsurumi, Kanagawa 230-0045, Japan4

Received 22 November 2004/ Accepted 12 May 2005

Sha (also known as Mrp/Mnh/Pha) is a Na+/H+ antiporter encoded by a cluster of six or seven genes that probably form a multisubunit transport complex. The Sha system is important for the homeostasis of H+, Na+, and other monovalent cations and plays a critical role in various functions, including alkaliphily, sporulation, and symbiosis. Here, we characterized the sha homologue genes from the opportunistic pathogen Pseudomonas aeruginosa, which exist as a cluster of six genes (PA1054 to PA1059). The gene cluster PA1054 to PA1059, but not the cluster with a deletion of PA1054, complemented a growth defect in the presence of 0.2 M NaCl and a defect in Na+/H+ antiport activity of the Escherichia coli TO114 mutant lacking the three major Na+/H+ antiporters, indicating that genes PA1054 to PA1059 are responsible for Na+/H+ antiport activity. We disrupted PA1054 (a shaA homologue gene) and determined its effect on Na+ tolerance during growth, Na+ efflux, and pathogenicity in mice. Disruption of PA1054 resulted in severe Na+ sensitivity during growth and decreased Na+ efflux activity. In mice, the deletion mutant of PA1054 also exhibited an attenuated virulence in systemic, pulmonary, and urinary tract infections and also a decrease in colonization of the infected organs. From these results, we conclude that the genes PA1054 to PA1059 encode a Na+/H+ antiporter that is largely responsible for Na+ extrusion in P. aeruginosa and has a role in the infection of the pathogen. We propose to designate PA1054 to PA1059 as the sha (sodium hydrogen antiporter) genes, shaABCDEFG.

* Corresponding author. Mailing address: Environmental Molecular Biology Laboratory, RIKEN, Wako, Saitama 351-0198, Japan. Phone: 81-48-467-9545. Fax: 81-48-462-4672. E-mail: kosono{at}riken.jp.

Journal of Bacteriology, August 2005, p. 5242-5248, Vol. 187, No. 15
0021-9193/05/$08.00+0     doi:10.1128/JB.187.15.5242-5248.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Fukaya, F., Promden, W., Hibino, T., Tanaka, Y., Nakamura, T., Takabe, T. (2009). An Mrp-Like Cluster in the Halotolerant Cyanobacterium Aphanothece halophytica Functions as a Na+/H+ Antiporter. Appl. Environ. Microbiol. 75: 6626-6629 [Abstract] [Full Text]  
  • Yamaguchi, T., Tsutsumi, F., Putnoky, P., Fukuhara, M., Nakamura, T. (2009). pH-dependent regulation of the multi-subunit cation/proton antiporter Pha1 system from Sinorhizobium meliloti. Microbiology 155: 2750-2756 [Abstract] [Full Text]  
  • Kajiyama, Y., Otagiri, M., Sekiguchi, J., Kudo, T., Kosono, S. (2009). The MrpA, MrpB and MrpD subunits of the Mrp antiporter complex in Bacillus subtilis contain membrane-embedded and essential acidic residues. Microbiology 155: 2137-2147 [Abstract] [Full Text]  
  • Morino, M., Natsui, S., Swartz, T. H., Krulwich, T. A., Ito, M. (2008). Single Gene Deletions of mrpA to mrpG and mrpE Point Mutations Affect Activity of the Mrp Na+/H+ Antiporter of Alkaliphilic Bacillus and Formation of Hetero-Oligomeric Mrp Complexes. J. Bacteriol. 190: 4162-4172 [Abstract] [Full Text]  
  • Swartz, T. H., Ito, M., Ohira, T., Natsui, S., Hicks, D. B., Krulwich, T. A. (2007). Catalytic Properties of Staphylococcus aureus and Bacillus Members of the Secondary Cation/Proton Antiporter-3 (Mrp) Family Are Revealed by an Optimized Assay in an Escherichia coli Host. J. Bacteriol. 189: 3081-3090 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»