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Journal of Bacteriology, October 2001, p. 5762-5767, Vol. 183, No. 19
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

Tatsunosuke Nakamura,1,* Yumiko Fujisaki,1 Hiromi Enomoto,1 Yuji Nakayama,1 Teruhiro Takabe,2 Naoto Yamaguchi,1 and Nobuyuki Uozumi3

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.


* 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.


Journal of Bacteriology, October 2001, p. 5762-5767, Vol. 183, No. 19
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.19.5762-5767.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



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