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
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.
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收藏
页码:469 / 476
页数:7
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