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

被引:0
作者
Crowell, DN [1 ]
Kennedy, M [1 ]
机构
[1] Indiana Univ Purdue Univ, Dept Biol, Indianapolis, IN 46202 USA
关键词
Arabidopsis thaliana; protein isoprenylation; protein methylation; yeast complementation;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:469 / 476
页数:8
相关论文
共 44 条
[1]  
ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999
[2]  
BERANGER F, 1994, J BIOL CHEM, V269, P13637
[4]   Prenylcysteine α-carboxyl methyltransferase in suspension-cultured tobacco cells [J].
Crowell, DN ;
Sen, SE ;
Randall, SK .
PLANT PHYSIOLOGY, 1998, 118 (01) :115-123
[5]   A protein farnesyl transferase involved in abscisic acid signal transduction in Arabidopsis [J].
Cutler, S ;
Ghassemian, M ;
Bonetta, D ;
Cooney, S ;
McCourt, P .
SCIENCE, 1996, 273 (5279) :1239-1241
[6]   Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum [J].
Dai, Q ;
Choy, E ;
Chiu, V ;
Romano, J ;
Slivka, SR ;
Steitz, SA ;
Michaelis, S ;
Philips, MR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (24) :15030-15034
[7]   The carboxyl methyltransferase modifying G proteins is a metalloenzyme [J].
Desrosiers, RR ;
Nguyen, QT ;
Béliveau, R .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1999, 261 (03) :790-797
[8]   PRENYL PROTEINS IN EUKARYOTIC CELLS - A NEW TYPE OF MEMBRANE ANCHOR [J].
GLOMSET, JA ;
GELB, MH ;
FARNSWORTH, CC .
TRENDS IN BIOCHEMICAL SCIENCES, 1990, 15 (04) :139-142
[9]   ALL RAS PROTEINS ARE POLYISOPRENYLATED BUT ONLY SOME ARE PALMITOYLATED [J].
HANCOCK, JF ;
MAGEE, AI ;
CHILDS, JE ;
MARSHALL, CJ .
CELL, 1989, 57 (07) :1167-1177
[10]   METHYLATION AND PROTEOLYSIS ARE ESSENTIAL FOR EFFICIENT MEMBRANE-BINDING OF PRENYLATED P21K-RAS(B) [J].
HANCOCK, JF ;
CADWALLADER, K ;
MARSHALL, CJ .
EMBO JOURNAL, 1991, 10 (03) :641-646