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Plant Physiol, April 2000, Vol. 122, pp. 1249-1260

The Arabidopsis HKT1 Gene Homolog Mediates Inward Na+ Currents in Xenopus laevis Oocytes and Na+ Uptake in Saccharomyces cerevisiae1

Nobuyuki Uozumi, Eugene J. Kim, Francisco Rubio,2 Takao Yamaguchi, Shoshi Muto, Akio Tsuboi, Evert P. Bakker, Tatsunosuke Nakamura, and Julian I. Schroeder

Bioscience Center, Nagoya University, Nagoya, 464-8601, Japan (N.U., S.M.); Department of Biology and Center for Molecular Genetics, University of California at San Diego, La Jolla, California 92093-0116 (N.U., E.J.K., F.R., J.I.S.); Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601, Japan (N.U., T.Y., S.M.); Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan (A.T.); Abteilung Mikrobiologie, Universität Osnabrück, Barbarastrasse 11, D-49076 Osnabrück, Germany (E.P.B.); and Faculty of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan (T.N.)

The Na+-K+ co-transporter HKT1, first isolated from wheat, mediates high-affinity K+ uptake. The function of HKT1 in plants, however, remains to be elucidated, and the isolation of HKT1 homologs from Arabidopsis would further studies of the roles of HKT1 genes in plants. We report here the isolation of a cDNA homologous to HKT1 from Arabidopsis (AtHKT1) and the characterization of its mode of ion transport in heterologous systems. The deduced amino acid sequence of AtHKT1 is 41% identical to that of HKT1, and the hydropathy profiles are very similar. AtHKT1 is expressed in roots and, to a lesser extent, in other tissues. Interestingly, we found that the ion transport properties of AtHKT1 are significantly different from the wheat counterpart. As detected by electrophysiological measurements, AtHKT1 functioned as a selective Na+ uptake transporter in Xenopus laevis oocytes, and the presence of external K+ did not affect the AtHKT1-mediated ion conductance (unlike that of HKT1). When expressed in Saccharomyces cerevisiae, AtHKT1 inhibited growth of the yeast in a medium containing high levels of Na+, which correlates to the large inward Na+ currents found in the oocytes. Furthermore, in contrast to HKT1, AtHKT1 did not complement the growth of yeast cells deficient in K+ uptake when cultured in K+-limiting medium. However, expression of AtHKT1 did rescue Escherichia coli mutants carrying deletions in K+ transporters. The rescue was associated with a less than 2-fold stimulation of K+ uptake into K+-depleted cells. These data demonstrate that AtHKT1 differs in its transport properties from the wheat HKT1, and that AtHKT1 can mediate Na+ and, to a small degree, K+ transport in heterologous expression systems.


1 This work was supported by the U.S. Department of Agriculture (grant no. 98-3504-6684 to J.I.S.), by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan (nos. 11660082 and 11132227 to N.U.), and by the Salt Science Research Foundation Grant. This work was also supported in part by a U.S. Department of Agriculture Postdoctoral Fellowship (no. 9801009 to E.J.K.), by the Deutshe Forschungsgemeinschaft (no. SFB431 to E.P.B), and by the Fonds der Chemischen Industrie (to E.P.B.).

2 Present address: Departemento de Biotecnologia, Escuela Tecnica Superior de Ingenierous Agronomos, 28040 Madrid, Spain.

© 2000 American Society of Plant Physiologists



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