Plant PRMTs Broaden the Scope of Arginine Methylation

Ayaz Ahmad; Xiaofeng Cao

doi:10.1016/j.jgg.2012.04.001

Volume 39 Issue 5

May 2012

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Article Navigation > Journal of Genetics and Genomics > 2012 > 39(5): 195-208

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Plant PRMTs Broaden the Scope of Arginine Methylation

doi: 10.1016/j.jgg.2012.04.001

Ayaz Ahmad^{a, b},
Xiaofeng Cao^a

a
State Key Laboratory of Plant Genomics and National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Datun Road #5, Beijing 100101, China
b
Graduate University of the Chinese Academy of Sciences, Yuquan Road, Beijing 100039, China

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Corresponding author: E-mail address: xfcao@genetics.ac.cn (Xiaofeng Cao)
Received Date: 2012-02-29
Accepted Date: 2012-04-02
Rev Recd Date: 2012-04-02

Available Online: 2012-04-11

Publish Date: 2012-05-20

Abstract

Abstract

Post-translational methylation at arginine residues is one of the most important covalent modifications of proteins, involved in a myriad of essential cellular processes in eukaryotes, such as transcriptional regulation, RNA processing, signal transduction, and DNA repair. Methylation at arginine residues is catalyzed by a family of enzymes called protein arginine methyltransferases (PRMTs). PRMTs have been extensively studied in various taxa and there is a growing tendency to unveil their functional importance in plants. Recent studies in plants revealed that this evolutionarily conserved family of enzymes regulates essential traits including vegetative growth, flowering time, circadian cycle, and response to high medium salinity and ABA. In this review, we highlight recent advances in the field of post-translational arginine methylation with special emphasis on the roles and future prospects of this modification in plants.
- PRMTs,
- Post-translational modifications,
- Arginine methylation

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References(123)

References

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