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Originally published In Press as doi:10.1074/jbc.M001112200 on July 19, 2000
J. Biol. Chem., Vol. 275, Issue 39, 30287-30292, September 29, 2000
Bacillus subtilis YqkI Is a Novel
Malic/Na+-Lactate Antiporter That Enhances Growth on Malate
at Low Protonmotive Force*
Yi
Wei ,
Arthur A.
Guffanti ,
Masahiro
Ito§, and
Terry A.
Krulwich ¶
From the Department of Biochemistry and Molecular
Biology, Mount Sinai School of Medicine, New York, New York 10029 and § Department of Life Science, Toyo University,
Oura-gun, Gunma 374-0193, Japan
Bacillus subtilis yheL encodes a
Na+/H+ antiporter, whereas its paralogue,
yqkI, encodes a novel antiporter that achieves a simultaneous Na+/H+ and malolactate
antiport. B. subtilis yufR, a control in some experiments, encodes a Na+/malate symporter. YqkI
complemented a malate transport mutant of Escherichia coli
if Na+ and lactate were present. YheL conferred
Na+ uptake capacity on everted membrane vesicles from an
antiporter-deficient E. coli mutant that was consistent
with a secondary Na+/H+ antiport, but
YqkI-dependent Na+ uptake depended on
intravesicular malate and extravesicular lactate. YqkI-dependent lactate uptake depended on intravesicular
malate and extravesicular Na+. YqkI mediated an
electroneutral exchange, which is proposed to be a
malic 2-2H+ (or fully protonated
malate)/Na+-lactate 1 antiport. Because the
composite YqkI-mediated exchanges could be driven by gradients of the
malate-lactate pair, this transporter could play a role in growth of
B. subtilis on malate at low protonmotive force. A mutant
with a disruption of yqkI exhibited an abrupt arrest in the
mid-logarithmic phase of growth on malate when low concentrations of
protonophore were present. Thus growth of B. subtilis to
high density on a putatively nonfermentative dicarboxylic acid
substrate depends on a malolactate exchange at suboptimal protonmotive force.
*
This work was supported by Research Grants GM52837 and
GM28454 from the National Institutes of General Medical Sciences (to T. A. K.) and by The Inoue Enryo Memorial Foundation for Promoting Science (to M. I.).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: Box 1020, Dept. of
Biochemistry & Molecular Biology, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029. Tel.: 212-241-7280; Fax:
212-241-996-7214; E-mail: terry.krulwich@mssm.edu.
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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