Mutational analysis of amiloride sensitivity of the NhaA Na+/H+ antiporter from Vibrio parahaemolyticus

T. Kuroda, T. Shimamoto, T. Mizushima, T. Tsuchiya

研究成果: Article

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The activity of the NhaA Na+/H+ antiporter of Vibrio parahaemolyticus is inhibited by amiloride. We found an amino acid sequence in the NhaA that was identical to a putative amiloride binding domain of the Na+/H+ exchanger in mammalian cells. We constructed mutant NhaAs that had amino acid substitutions in the putative amiloride binding domain by site-directed mutagenesis. These include V62L (Val62 replaced by Leu), F63Y, F64Y, and L65F. Most mutant NhaAs showed decreased sensitivity for amiloride. Among these, the F64Y mutant NhaA showed the least amiloride sensitivity, with a K(i) value 7 to 10 times greater than that in the wild type. Thus, the sequence between residues V62 and L65 in NhaA, especially F64, is very important for the inhibitory effect of amiloride on the antiporter.

元の言語English
ページ(範囲)7600-7602
ページ数3
ジャーナルJournal of Bacteriology
179
発行部数23
DOI
出版物ステータスPublished - 1997 1 1

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ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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