Crowell D N, Kennedy M
Department of Biology, Indiana University-Purdue University at Indianapolis, 46202-5132, USA.
Plant Mol Biol. 2001 Mar;45(4):469-76. doi: 10.1023/a:1010671202925.
Most isoprenylated proteins are alpha-carboxyl-methylated. However, despite numerous studies linking protein isoprenylation in plants to cell cycle control, meristem development, and phytohormone signaling, alpha-carboxyl methylation of isoprenylated plant proteins has not been characterized in detail. Here, we report the cloning of a prenylcysteine alpha-carboxyl methyltransferase gene (AtSTE14) from Arabidopsis thaliana. AtSTE14 restores fertility and enzymatic activity to a ste14 mutant of Saccharomyces cerevisiae, confirming its identity as a bona fide prenylcysteine alpha-carboxyl methyltransferase gene. Furthermore, the presence of AtSTE14 transcripts in various Arabidopsis organs suggests a ubiquitous role for the AtSTE14 protein in plant growth and development. These results demonstrate that Arabidopsis thaliana possesses a functional prenylcysteine alpha-carboxyl methyltransferase involved in post-isoprenylation protein processing.
大多数异戊二烯化蛋白都进行了α-羧甲基化修饰。然而,尽管有大量研究将植物中的蛋白异戊二烯化与细胞周期调控、分生组织发育以及植物激素信号传导联系起来,但异戊二烯化植物蛋白的α-羧甲基化尚未得到详细表征。在此,我们报道了从拟南芥中克隆出一个异戊烯基半胱氨酸α-羧甲基转移酶基因(AtSTE14)。AtSTE14可恢复酿酒酵母ste14突变体的育性和酶活性,证实其作为一个真正的异戊烯基半胱氨酸α-羧甲基转移酶基因的身份。此外,AtSTE14转录本在拟南芥各个器官中的存在表明AtSTE14蛋白在植物生长发育中具有普遍作用。这些结果表明拟南芥拥有一种参与异戊二烯化后蛋白加工的功能性异戊烯基半胱氨酸α-羧甲基转移酶。