Identification and functional expression in yeast of a prenylcysteine α-carboxyl methyltransferase gene from Arabidopsis thaliana

被引：14

作者：

N. Crowell D. ^{[1
]}

Kennedy M. ^{[1
,2
]}

机构：

[1] Department of Biology, Indiana University-Purdue University at Indianapolis, Indianapolis, IN 46202-5132

[2] Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, CA 90095

来源：

Crowell, D.N. (dcrowell@iupui.edu) | 2001年 / Kluwer Academic Publishers卷 / 45期

关键词：

Arabidopsis thaliana; Protein isoprenylation; Protein methylation; Yeast complementation;

D O I：

10.1023/A:1010671202925

中图分类号：

学科分类号：

摘要：

Most isoprenylated proteins are α-carboxyl-methylated. However, despite numerous studies linking protein isoprenylation in plants to cell cycle control, meristem development, and phytohormone signaling, α-carboxyl methylation of isoprenylated plant proteins has not been characterized in detail. Here, we report the cloning of a prenylcysteine α-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 α-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 α-carboxyl methyltransferase involved in post-isoprenylation protein processing.

引用

页码：469 / 476

页数：7

共 44 条

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