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J. Biol. Chem., Vol. 275, Issue 26, 20223-20228, June 30, 2000
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From the Division of Biological Science, Graduate School of
Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan
Four integral membrane proteins, PomA, PomB,
MotX, and MotY, are thought to be directly involved in torque
generation of the Na+-driven polar flagellar motor of
Vibrio alginolyticus. Our previous study showed that PomA
and PomB form a complex, which catalyzes sodium influx in response to a
potassium diffusion potential. PomA forms a stable dimer when expressed
in a PomB null mutant. To explore the possible functional dependence of
PomA domains in adjacent subunits, we prepared a series of PomA dimer
fusions containing different combinations of wild-type or mutant
subunits. Introduction of the mutation P199L, which completely
inactivates flagellar rotation, into either the first or the second
half of the dimer abolished motility. The P199L mutation in monomeric PomA also altered the PomA-PomB interaction. PomA dimer with the P199L
mutation even in one subunit also had no ability to interact with PomB,
indicating that the both subunits in the dimer are required for the
functional interaction between PomA and PomB. Flagellar rotation by
wild-type PomA dimer was completely inactivated by phenamil, a sodium
channel blocker. However, activity was retained in the presence of
phenamil when either half of the dimer was replaced with a
phenamil-resistant subunit, indicating that both subunits must bind
phenamil for motility to be fully inhibited. These observations
demonstrate that both halves of the PomA dimer function together to
generate the torque for flagellar rotation.
Multimeric Structure of PomA, a Component of the
Na+-driven Polar Flagellar Motor of Vibrio
alginolyticus*
and
*
This study was supported by grants from 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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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