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    J Biol Chem. 1991 Jun 15;266(17):11289-94.

    Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli.

    Taglicht D, Padan E, Schuldiner S.

    Source

    Institute of Life Sciences, Hebrew University, Jerusalem, Israel.

    Abstract

    A Na+/H+ antiporter coded by the nhaA (ant) gene of Escherichia coli has been overproduced and purified. The amino-terminal sequence of the protein has been determined and shown to correlate with initiation at a GUG codon, 75 bases upstream from the previously suggested AUG initiation codon. The purified protein, when reconstituted into proteoliposomes, has Na+/H+ antiport activity. It can mediate sodium uptake when a transmembrane pH gradient is applied. Downhill sodium efflux is shown to be highly dependent on pH and is accelerated by a transmembrane pH gradient. An imposed membrane potential negative inside accelerates Na+ efflux at all pH values tested. These findings suggest that the antiporter is electrogenic both at acid and alkaline pH. The activation at alkaline pH values (2000-fold increase) is consistent with the proposed role of the antiporter in regulation of internal pH at the alkaline pH range.

    PMID:
    1645730
    [PubMed - indexed for MEDLINE]

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