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 Ohyama, T Articles by Kobayashi, H Search for Related Content PubMed PubMed Citation Articles by Ohyama, T Articles by Kobayashi, H

 Previous Article  |  Next Article 

J Bacteriol. 1994 July; 176(14): 4311-4315

research-article

Physiological role of the chaA gene in sodium and calcium circulations at a high pH in Escherichia coli.

Faculty of Pharmaceutical Sciences, Chiba University, Japan.

ABSTRACT

Ohyama et al. previously isolated Escherichia coli mutant RS1, which had a negligible activity for sodium ion extrusion at alkaline pH (T. Ohyama, R. Imaizumi, K. Igarashi, and H. Kobayashi, J. Bacteriol. 174:7743-7749, 1992). Our present study showed that the mutation of RS1 was compensated for by a cloned chaA gene. It has been proposed that sodium ion extrusion by ChaA is prevented under physiological conditions (D. M. Ivey, A. A. Guffanti, J. Zemsky, E. Pinner, R. Karpel, E. Padan, S. Schuldiner, and T. A. Krulwich, J. Biol. Chem. 268:11296-11303, 1993). In order to clarify the physiological role of chaA in sodium ion circulation at alkaline pH, we constructed a delta chaA mutant. The resultant mutant, TO112, deficient in both nhaA and chaA, was unable to grow at pH 8.5 in medium containing 0.1 M sodium chloride and had negligible sodium ion extrusion activity. However, TO112 grew at pH 7.0 in medium containing 0.4 M sodium chloride. Sodium ions were extruded from TO112 cells at neutral pH. The extrusion activity at pH 7.5 was greatly reduced by the deletion of nhaB. These data demonstrate that the activity of nhaB is low at high pH and that ChaA extrudes sodium ions at alkaline pH. The uptake of calcium ions by everted membrane vesicles prepared from the delta chaA mutant TO110 was 60% of the activity observed in the vesicles of the wild-type strain at pH 8.5, but the activity at neutral pH was not reduced by the deletion of chaA. Therefore, it was also suggested that ChaA plays a role in calcium ion circulation at alkaline pH.

This article has been cited by other articles:

• Billini, M., Stamatakis, K., Sophianopoulou, V. (2008). Two Members of a Network of Putative Na+/H+ Antiporters Are Involved in Salt and pH Tolerance of the Freshwater Cyanobacterium Synechococcus elongatus. J. Bacteriol. 190: 6318-6329 [Abstract] [Full Text]  
• Uddin, Md. I., Qi, Y., Yamada, S., Shibuya, I., Deng, X.-P., Kwak, S.-S., Kaminaka, H., Tanaka, K. (2008). Overexpression of a New Rice Vacuolar Antiporter Regulating Protein OsARP Improves Salt Tolerance in Tobacco. Plant Cell Physiol 49: 880-890 [Abstract] [Full Text]  
• Wei, Y., Liu, J., Ma, Y., Krulwich, T. A. (2007). Three putative cation/proton antiporters from the soda lake alkaliphile Alkalimonas amylolytica N10 complement an alkali-sensitive Escherichia coli mutant. Microbiology 153: 2168-2179 [Abstract] [Full Text]  
• Radchenko, M. V., Tanaka, K., Waditee, R., Oshimi, S., Matsuzaki, Y., Fukuhara, M., Kobayashi, H., Takabe, T., Nakamura, T. (2006). Potassium/Proton Antiport System of Escherichia coli. J. Biol. Chem. 281: 19822-19829 [Abstract] [Full Text]  
• Liu, J., Xue, Y., Wang, Q., Wei, Y., Swartz, T. H., Hicks, D. B., Ito, M., Ma, Y., Krulwich, T. A. (2005). The Activity Profile of the NhaD-Type Na+(Li+)/H+ Antiporter from the Soda Lake Haloalkaliphile Alkalimonas amylolytica Is Adaptive for the Extreme Environment. J. Bacteriol. 187: 7589-7595 [Abstract] [Full Text]  
• Matsuda, N., Kobayashi, H., Katoh, H., Ogawa, T., Futatsugi, L., Nakamura, T., Bakker, E. P., Uozumi, N. (2004). Na+-dependent K+ Uptake Ktr System from the Cyanobacterium Synechocystis sp. PCC 6803 and Its Role in the Early Phases of Cell Adaptation to Hyperosmotic Shock. J. Biol. Chem. 279: 54952-54962 [Abstract] [Full Text]  
• Cai, X., Lytton, J. (2004). The Cation/Ca2+ Exchanger Superfamily: Phylogenetic Analysis and Structural Implications. Mol Biol Evol 21: 1692-1703 [Abstract] [Full Text]  
• Nakamura, T., Fujisaki, Y., Enomoto, H., Nakayama, Y., Takabe, T., Yamaguchi, N., Uozumi, N. (2001). Residue Aspartate-147 from the Third Transmembrane Region of Na+/H+ Antiporter NhaB of Vibrio alginolyticus Plays a Role in Its Activity. J. Bacteriol. 183: 5762-5767 [Abstract] [Full Text]  
• Inaba, M., Sakamoto, A., Murata, N. (2001). Functional Expression in Escherichia coli of Low-Affinity and High-Affinity Na+(Li+)/H+ Antiporters of Synechocystis. J. Bacteriol. 183: 1376-1384 [Abstract] [Full Text]  
• Hamada, A., Hibino, T., Nakamura, T., Takabe, T. (2001). Na+/H+ Antiporter from Synechocystis Species PCC 6803, Homologous to SOS1, Contains an Aspartic Residue and Long C-Terminal Tail Important for the Carrier Activity. Plant Physiol. 125: 437-446 [Abstract] [Full Text]  
• Wood, J. M. (1999). Osmosensing by Bacteria: Signals and Membrane-Based Sensors. Microbiol. Mol. Biol. Rev. 63: 230-262 [Abstract] [Full Text]  
• Kakinuma, Y. (1998). Inorganic Cation Transport and Energy Transduction in Enterococcus hirae and Other Streptococci. Microbiol. Mol. Biol. Rev. 62: 1021-1045 [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]  
• Williams, S. G., Carmel-Harel, O., Manning, P. A. (1998). A Functional Homolog of Escherichia coli NhaR in Vibrio cholerae. J. Bacteriol. 180: 762-765 [Abstract] [Full Text]  
• Harel-Bronstein, M., Dibrov, P., Olami, Y., Pinner, E., Schuldiner, S., Padan, E. (1995). MH1, A Second-site Revertant of an Escherichia coli Mutant Lacking Na[IMAGE]/H[IMAGE] Antiporters (DeltanhaADeltanhaB), Regains Na[IMAGE] Resistance and a Capacity to Excrete Na[IMAGE] in a Deltat;ex2html_html_special_mark_amp;mgr;[IMAGE]-independent Fashion. J. Biol. Chem. 270: 3816-3822 [Abstract] [Full Text]  
• Waditee, R., Hibino, T., Tanaka, Y., Nakamura, T., Incharoensakdi, A., Takabe, T. (2001). Halotolerant Cyanobacterium Aphanothece halophytica Contains an Na+/H+ Antiporter, Homologous to Eukaryotic Ones, with Novel Ion Specificity Affected by C-terminal Tail. J. Biol. Chem. 276: 36931-36938 [Abstract] [Full Text]