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J Biol Chem, Vol. 275, Issue 8, 5718-5722, February 25, 2000

Functional Reconstitution of the Na+-driven Polar Flagellar Motor Component of Vibrio alginolyticus*

Ken SatoDagger and Michio Homma

From the Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan

The bacterial flagellar motor is a molecular machine that couples the influx of specific ions to the generation of the force necessary to drive rotation of the flagellar filament. Four integral membrane proteins, PomA, PomB, MotX, and MotY, have been suggested to be directly involved in torque generation of the Na+-driven polar flagellar motor of Vibrio alginolyticus. In the present study, we report the isolation of the functional component of the torque-generating unit. The purified protein complex appears to consist of PomA and PomB and contains neither MotX nor MotY. The PomA/B protein, reconstituted into proteoliposomes, catalyzed 22Na+ influx in response to a potassium diffusion potential. Sodium uptake was abolished by the presence of Li+ ions and phenamil, a sodium channel blocker. This is the first demonstration of a purification and functional reconstitution of the bacterial flagellar motor component involved in torque generation. In addition, this study demonstrates that the Na+-driven motor component, PomA and PomB, forms the Na+-conducting channel.


* This study was supported by grants from the Ministry of Education, Science, Sports and Culture of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Tel.: 81-52-789-2992; Fax: 81-52-789-3001; E-mail: m47004a@nucc.cc.nagoya-u.ac.jp.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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