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Journal of Bacteriology, January 2005, p. 388-391, Vol. 187, No. 1
0021-9193/05/$08.00+0     doi:10.1128/JB.187.1.388-391.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Mrp Na+/H+ Antiporter Increases the Activity of the Malate:Quinone Oxidoreductase of an Escherichia coli Respiratory Mutant

Talia H. Swartz,1 Masahiro Ito,2 David B. Hicks,1 Mark Nuqui,1 Arthur A. Guffanti,1 and Terry A. Krulwich1*

Department of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, New York, New York,1 Department of Life Sciences, Toyo University, Itakura-machi, Gunma, Japan2

Received 23 August 2004/ Accepted 29 September 2004

Mrp catalyzes secondary Na+/H+ antiport and was hypothesized to have an additional primary energization mode. Mrp-dependent complementation of nonfermentative growth of an Escherichia coli respiratory mutant supported this hypothesis but is shown here to be related to increased expression of host malate:quinone oxidoreductase, not to catalytic activity of Mrp.

* Corresponding author. Mailing address: Box 1603, Department of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029. Phone: (212) 241-7280. Fax: (212) 996-7214. E-mail: terry.krulwich{at}mssm.edu.

Journal of Bacteriology, January 2005, p. 388-391, Vol. 187, No. 1
0021-9193/05/$08.00+0     doi:10.1128/JB.187.1.388-391.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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