Identification and functional expression in yeast of a prenylcysteine α-carboxyl methyltransferase gene from Arabidopsis thaliana
被引:14
|
作者:
N. Crowell D.
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机构:
Department of Biology, Indiana University-Purdue University at Indianapolis, Indianapolis, IN 46202-5132Department of Biology, Indiana University-Purdue University at Indianapolis, Indianapolis, IN 46202-5132
N. Crowell D.
[1
]
Kennedy M.
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机构:
Department of Biology, Indiana University-Purdue University at Indianapolis, Indianapolis, IN 46202-5132
Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, CA 90095Department of Biology, Indiana University-Purdue University at Indianapolis, Indianapolis, IN 46202-5132
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
Arabidopsis thaliana;
Protein isoprenylation;
Protein methylation;
Yeast complementation;
D O I:
10.1023/A:1010671202925
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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.