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

[1]

Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J., Basic local alignment search tool, J. Mol. Biol., 215, pp. 403-410, (1990)

[2]

Beranger F., Cadwallader K., Porfiri E., Powers S., Evans T., De Gunzberg J., Hancock J.F., Determination of structural requirements for the interaction of Rab6 with RabGDI and Rab geranylgeranyltransferase, J. Biol. Chem., 269, pp. 13637-13643, (1994)

[3]

Clarke S., Protein isoprenylation and methylation at carboxyl-terminal cysteine residues, Annu. Rev. Biochem., 61, pp. 355-386, (1992)

[4]

Crowell D.N., Sen S.E., Randall S.K., Prenylcysteine α-carboxyl methyltransferase in suspension-cultured tobacco cells, Plant Physiol., 118, pp. 115-123, (1998)

[5]

Cutler S., Ghassemian M., Bonetta D., Cooney S., McCourt P., A protein farnesyl transferase involved in abscisic acid signal transduction in Arabidopsis, Science, 273, pp. 1239-1241, (1996)

[6]

Dai Q., Choy E., Chiu V., Romano J., Slivka S.R., Steitz S.A., Michaelis S., Philips M.R., Mammalian prenylcysteine carboxyl methyltransferase is the endoplasmic reticulum, J. Biol. Chem., 273, pp. 15030-15034, (1998)

[7]

Desrosiers R.R., Nguyen Q.T., Beliveau R., The carboxyl methyltransferase modifying G proteins is a metalloenzyme, Biochem. Biophys. Res. Commun., 261, pp. 790-797, (1999)

[8]

Glomset J.A., Gelb M.H., Farnsworth C.C., Prenyl proteins in eukaryotic cells: A new type of membrane anchor, Trends Biochem. Sci., 15, pp. 139-142, (1990)

[9]

Hancock J.F., Cadwallader K., Marshall C.J., Methylation and proteolysis are essential for efficient membrane binding of prenylated p21<sup>K-ras(B)</sup>, EMBO J., 10, pp. 641-646, (1991)

[10]

Hancock J.F., Magee A.I., Childs J.E., Marshall C.J., All ras proteins are polyisoprenylated but only some are palmitoylated, Cell, 57, pp. 1167-1177, (1989)

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