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

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

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)7600-7602
Number of pages3
JournalJournal of bacteriology
Volume179
Issue number23
DOIs
Publication statusPublished - Jan 1 1997

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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