鉴定小鼠无眼 3 蛋白的苏氨酸磷酸酶。

Characterization of the threonine-phosphatase of mouse eyes absent 3.

机构信息

Department of Medical Chemistry, Graduate School of Medicine, Kyoto University, Yoshida-Konoe, Kyoto, Japan.

出版信息

FEBS Lett. 2011 Sep 2;585(17):2714-9. doi: 10.1016/j.febslet.2011.07.029. Epub 2011 Aug 2.

DOI:10.1016/j.febslet.2011.07.029

Abstract

Eyes absent (EYA) has tyrosine- and threonine-phosphatase activities in their C-terminal and N-terminal regions, respectively. Using various mutants of mouse EYA3, we showed that the 68-amino acid domain between positions 53 and 120 was necessary and sufficient for its threonine-phosphatase activity. Point mutations were then introduced, and residues Cys-56, Tyr-77, His-79, and Tyr-90 were essential for the EYA3s threonine-phosphatase. The 68-amino acid domain is not well conserved among the four mouse EYA members, but is evolutionally highly conserved in the orthologous EYA members of different species, suggesting that the threonine-phosphatase of EYA3 has a function distinct from that of the other EYAs.

摘要

EYA（眼睛缺失）在其 C 末端和 N 末端区域分别具有酪氨酸和苏氨酸磷酸酶活性。利用小鼠 EYA3 的各种突变体，我们表明，位置 53 和 120 之间的 68 个氨基酸域对于其苏氨酸磷酸酶活性是必需且充分的。然后引入点突变，残基 Cys-56、Tyr-77、His-79 和 Tyr-90 对于 EYA3 的苏氨酸磷酸酶是必需的。在这四个小鼠 EYA 成员中，68 个氨基酸域没有很好地保守，但在不同物种的同源 EYA 成员中进化上高度保守，这表明 EYA3 的苏氨酸磷酸酶具有与其他 EYAs 不同的功能。