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Journal of Bacteriology, January 2003, p. 674-678, Vol. 185, No. 2
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.2.674-678.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Experimental Verification of a Sequence-Based Prediction: F₁F₀-Type ATPase of Vibrio cholerae Transports Protons, Not Na⁺ Ions

Department of Microbiology, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada,¹ Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105,² National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894³

Received 10 June 2002/ Accepted 25 October 2002

The membrane energetics of the intestinal pathogen Vibrio cholerae involves both H⁺ and Na⁺ as coupling ions. The sequence of the c subunit of V. cholerae F₀F₁ ATPase suggested that this enzyme is H⁺ specific, in contrast to the results of previous studies on the Na⁺-dependent ATP synthesis in closely related Vibrio spp. Measurements of the pH gradient and membrane potential in membrane vesicles isolated from wild-type and atpE mutant V. cholerae show that the F₁F₀ ATPase of V. cholerae is an H⁺, not Na⁺, pump, confirming the bioinformatics assignments that were based on the Na⁺-binding model of S. Rahlfs and V. Müller (FEBS Lett. 404:269-271, 1999). Application of this model to the AtpE sequences from other bacteria and archaea indicates that Na⁺-specific F₁F₀ ATPases are present in a number of important bacterial pathogens.

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