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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
Sato 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.
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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Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
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