Molecular mechanism of aluminum-activated malate transporter

分析了小麦铝激活苹果酸转运蛋白(ALMT1)的表达和功能机制。我们证明了ALMT1上游序列的变化与小麦对铝的敏感性密切相关，并且ALMT1的亲水性C-末端结构域中的三个酸性氨基酸是铝激活运输功能所必需的。此外，我们还发现拟南芥中几个ALMT同系物的功能与铝抗性和气孔关闭有关，这表明ALMT蛋白由一个阴离子转运蛋白家族组成，具有不同的功能。

The mechanisms for the expression and function of aluminum-activated malate transporter (ALMT1) of wheat were analyzed. We demonstrated that the variation of the upstream sequence of ALMT1 is strongly correlated to the aluminum sensitivity of wheat, and that three acidic amino acids within hydrophilic C-terminal domain of ALMT1 is required for the activation of transport function by aluminum. Furthermore, we found that the functions of several ALMT homologues in Arabidopsis are related to aluminum resistance and closing stomata, suggesting that ALMT proteins comprise a family of anion transporters, possessing diverse functions.