Meyer Andreas, Eskandari Sepehr, Grallath Silke, Rentsch Doris
Institute of Plant Sciences, University of Bern, Altenbergrain 21, 3013 Bern, Switzerland.
J Biol Chem. 2006 Mar 17;281(11):7197-204. doi: 10.1074/jbc.M510766200. Epub 2006 Jan 10.
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 gamma-aminobutyric acid (GABA) transporter. In addition to GABA, other omega-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.
在异源表达系统(即酿酒酵母和非洲爪蟾卵母细胞)中对拟南芥GAT1进行功能表征,结果表明AtGAT1(At1g08230)编码一种由H⁺驱动的高亲和力γ-氨基丁酸(GABA)转运体。除GABA外,还可识别其他ω-氨基脂肪酸和丁胺。与脯氨酸转运体家族关系最密切的蛋白质不同,脯氨酸和甘氨酸甜菜碱不能被AtGAT1转运。AtGAT1与目前已描述的任何非植物GABA转运体均无序列相似性,对底物选择性和动力学特性的分析表明,AtGAT1介导的转运与哺乳动物、细菌和酿酒酵母的GABA转运体相似但不同。与GABA摄取进入细胞的作用一致,AtGAT1/绿色荧光蛋白融合蛋白在烟草原生质体中的瞬时表达显示其定位于质膜。在植物中,AtGAT1在花中以及在GABA浓度升高的条件下(如受伤或衰老)表达最高。