XXIth YGM Conference
Göteborg, Sweden
July 7-12th, 2003

Conference Web Site ( http://www.yeast2003.se )


Presenter's URL : http://sun2.biomed.cas.cz/fgu/


Abstract 13-1

Functional expression of the Oryza sativa NHX1 antiporter in Saccharomyces cerevisiae.
Olga Kinclova, Hana Flegelova, Hana Sychrova
Dept. Membrane Transport, Institute of Physiology, Videnska 1083, Prague 4 - Krc, 142 20, Czech Republic (kinclova@biomed.cas.cz)

Na+/H+ antiporters have been found in a wide variety of organisms. Their main role is to eliminate high toxic concentrations of Na+ and Li+ from cytosol by pumping the alkali metal cations out of cells or by sequestration in some compartments, e.g. vacuole. The O. sativa NHX1 gene encodes a Na+/H+ exchanger playing an important role in salt tolerance of rice. The OsNHX1 protein (535 aa) is similar to intracellularly localized antiporters from Arabidopsis thaliana (AtNhx1p, 73%) and S. cerevisiae (Nhx1p, 30%). To characterize transport properties and physiological role of the OsNHX1 antiporter, cDNA of OsNHX1 gene was expressed in a S. cerevisiae alkali-metal-cations-sensitive strain lacking its own Na+-transport systems (ena1-4 nha1 nhx1). Overexpression of OsNHX1 improved significantly the tolerance of S. cerevisiae mutant cells to Na+ and Li+, but not to K+. Microscopy analysis of the OsNHX1-GFP indicated its localization mainly in ER and vacuolar membranes of S. cerevisiae cells. Measurements of Na+/Li+ content and efflux in S. cerevisiae cells expressing OsNHX1 proved the antiporter's transport activity and substrate specificity. Functional expression of a plant antiporter in a yeast antiporter-less strain confirmed the suitability of yeast cells as a host system to study individual transport systems of higher eukaryots at the molecular level. This work was supported by grants from the Grant Agency of the Czech Republic (204/02/D092) and from the EU (QLK3-2001-00533).


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