Plant PRMTs Broaden the Scope of Arginine Methylation

被引:48
作者
Ahmad, Ayaz [1 ,2 ,3 ]
Cao, Xiaofeng [1 ,2 ]
机构
[1] Chinese Acad Sci, State Key Lab Plant Genom, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Natl Ctr Plant Gene Res, Beijing 100101, Peoples R China
[3] Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
基金
中国国家自然科学基金;
关键词
PRMTs; Post-translational modifications; Arginine methylation; RNA-POLYMERASE-II; N-METHYLTRANSFERASE; HISTONE H3; GENE-EXPRESSION; PROTEIN METHYLTRANSFERASE; SYMMETRIC DIMETHYLATION; CRYSTAL-STRUCTURE; DNA METHYLATION; FLOWERING TIME; IN-VIVO;
D O I
10.1016/j.jgg.2012.04.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
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.
引用
收藏
页码:195 / 208
页数:14
相关论文
共 123 条
[1]
Characterization of the PRMT Gene Family in Rice Reveals Conservation of Arginine Methylation [J].
Ahmad, Ayaz ;
Dong, Yuzhu ;
Cao, Xiaofeng .
PLOS ONE, 2011, 6 (08)
[2]
Decoding the Epigenetic Language of Plant Development [J].
Ahmad, Ayaz ;
Zhang, Yong ;
Cao, Xiao-Feng .
MOLECULAR PLANT, 2010, 3 (04) :719-728
[3]
Arginine methylation of SmB is required for Drosophila germ cell development [J].
Anne, Joel .
DEVELOPMENT, 2010, 137 (17) :2819-2828
[4]
PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits [J].
Bachand, F ;
Silver, PA .
EMBO JOURNAL, 2004, 23 (13) :2641-2650
[5]
Protein arginine methyltransferases: From unicellular eukaryotes to humans [J].
Bachand, Francois .
EUKARYOTIC CELL, 2007, 6 (06) :889-898
[6]
Regulation of chromatin by histone modifications [J].
Bannister, Andrew J. ;
Kouzarides, Tony .
CELL RESEARCH, 2011, 21 (03) :381-395
[7]
Methylation at arginine 17 of histone H3 is linked to gene activation [J].
Bauer, UM ;
Daujat, S ;
Nielsen, SJ ;
Nightingale, K ;
Kouzarides, T .
EMBO REPORTS, 2002, 3 (01) :39-44
[8]
Protein Arginine Methylation in Mammals: Who, What, and Why [J].
Bedford, Mark T. ;
Clarke, Steven G. .
MOLECULAR CELL, 2009, 33 (01) :1-13
[9]
Arginine methylation: An emerging regulator of protein function [J].
Bedford, MT ;
Richard, S .
MOLECULAR CELL, 2005, 18 (03) :263-272
[10]
Arginine methylation of RNA-binding proteins regulates cell function and differentiation [J].
Blackwell, Ernest ;
Ceman, Stephanie .
MOLECULAR REPRODUCTION AND DEVELOPMENT, 2012, 79 (03) :163-175