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Journal of Bacteriology, October 2001, p. 5762-5767, Vol. 183, No. 19
Laboratory of Molecular Cell Biology, Faculty
of Pharmaceutical Sciences, Chiba University, Inage-ku, Chiba
263-8522,1 Research Institute of Meijo
University, Tenpaku-ku, Nagoya, Aichi
468-8502,2 and Bioscience Center,
Nagoya University, Nagoya 464-8601,3 Japan
Received 30 April 2001/Accepted 10 July 2001
NhaB is a bacterial
Na+/H+ antiporter with
unique topology. The pH dependence of NhaB from Vibrio
alginolyticus differs from that of the Escherichia
coli NhaB homolog. Replacement of Asp-147 with Glu made high
H+ concentrations a requirement for the NhaB
activity. Replacement of Asp-147 with neutral amino acids inactivated NhaB.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.19.5762-5767.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Residue Aspartate-147 from the Third Transmembrane
Region of Na+/H+ Antiporter NhaB of
Vibrio alginolyticus Plays a Role in Its
Activity
*
Corresponding author. Mailing address: Laboratory of
Molecular Cell Biology, Faculty of Pharmaceutical Sciences, Chiba
University, 1-33, Yayoi-cho, Inage-ku, Chiba 263-8522, Japan. Phone:
(81) (43) 290 2932. Fax: (81) (43) 290 3021. E-mail:
tnakha{at}p.chiba-u.ac.jp.
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