PMID:1645730

Citation	Taglicht, D, Padan, E and Schuldiner, S (1991) Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli. J. Biol. Chem. 266:11289-94
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.
Links	PubMed
Keywords	Amino Acid Sequence; Base Sequence; Carrier Proteins/genetics; Carrier Proteins/isolation & purification; Carrier Proteins/metabolism; Cell Membrane/metabolism; Chromatography, Ion Exchange; Codon/genetics; Escherichia coli/genetics; Escherichia coli/metabolism; Genes, Bacterial; Hydrogen-Ion Concentration; Kinetics; Liposomes; Molecular Sequence Data; Plasmids; Proteolipids/metabolism; Sodium/metabolism; Sodium-Hydrogen Antiporter
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