Co-Authors:
Gaxiola, R.A., Whitehead Inst. for Biomed. Research, Massachusetts Inst. of Technology, 9 Cambridge Center, Cambridge, MA 02142-1479, United States
Rao, R., Johns Hopkins University, School of Medicine, Department of Physiology, 725 North Wolfe Street, Baltimore, MD 21205, United States
Sherman, A., Whitehead Inst. for Biomed. Research, Massachusetts Inst. of Technology, 9 Cambridge Center, Cambridge, MA 02142-1479, United States
Grisafi, P., Whitehead Inst. for Biomed. Research, Massachusetts Inst. of Technology, 9 Cambridge Center, Cambridge, MA 02142-1479, United States
Alper, S.L., Harvard Medical School, Molecular Medicine and Renal Units, RW763 Beth Israel Deaconess Med. C., 330 Brookline Avenue, Boston, MA 02215, United States
Fink, G.R., Whitehead Inst. for Biomed. Research, Massachusetts Inst. of Technology, 9 Cambridge Center, Cambridge, MA 02142-1479, United States
Abstract:
Overexpression of the Arabidopsis thaliana vacuolar H+-pyrophosphatase (AVP1) confers salt tolerance to the salt-sensitive ena1 mutant of Saccharomyces cerevisiae. Suppression of salt sensitivity requires two ion transporters, the Gef1 Cl- channel and the Nhx1 Na+/H+ exchanger. These two proteins colocalize to the prevacuolar compartment of yeast and are thought to be required for optimal acidification of this compartment. Overexpression of AtNHX1, the plant homologue of the yeast Na+/H+ exchanger, suppresses some of the mutant phenotypes of the yeast nhx1 mutant. Moreover, the level of AtNHX1 mRNA in Arabidopsis is increased in the presence of NaCl. The regulation of AtNHX1 by NaCl and the ability of the plant gene to suppress the yeast nhx1 mutant suggest that the mechanism by which cations are detoxified in yeast and plants may be similar.
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