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J. Biol. Chem., Vol. 281, Issue 11, 7197-7204, March 17, 2006

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AtGAT1, a High Affinity Transporter for -Aminobutyric Acid in Arabidopsis thaliana^*

Andreas Meyer, Sepehr Eskandari, Silke Grallath¹, and Doris Rentsch²

From the Institute of Plant Sciences, University of Bern, Altenbergrain 21, 3013 Bern, Switzerland and the Biological Sciences Department, California State Polytechnic University, Pomona, California 91768-4032

Functional characterization of Arabidopsis thaliana GAT1 in heterologous expression systems, i.e. Saccharomyces cerevisiae and Xenopus laevis oocytes, revealed that AtGAT1 (At1g08230) codes for an H⁺-driven, high affinity -aminobutyric acid (GABA) transporter. In addition to GABA, other -aminofatty acids and butylamine are recognized. In contrast to the most closely related proteins of the proline transporter family, proline and glycine betaine are not transported by AtGAT1. AtGAT1 does not share sequence similarity with any of the non-plant GABA transporters described so far, and analyses of substrate selectivity and kinetic properties showed that AtGAT1-mediated transport is similar but distinct from that of mammalian, bacterial, and S. cerevisiae GABA transporters. Consistent with a role in GABA uptake into cells, transient expression of AtGAT1/green fluorescent protein fusion proteins in tobacco protoplasts revealed localization at the plasma membrane. In planta, AtGAT1 expression was highest in flowers and under conditions of elevated GABA concentrations such as wounding or senescence.

Received for publication, October 3, 2005 , and in revised form, December 26, 2005.

^* This work was supported by Grants 31-64918.01 and 3100A0-107507 from the Swiss National Foundation (to A. M., S. G., and D. R.) and National Institutes of Health Grant S06 GM53933 (to S. E.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: Max-Planck-Institut für Biochemie, Zelluläre Biochemie, 82152 Martinsried, Germany.

² To whom correspondence should be addressed. Tel.: 41-31-631-4916; Fax: 41-31-631-4942; E-mail: doris.rentsch{at}ips.unibe.ch.

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