title: Plant PRMTs broaden the scope of arginine methylation.
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.
authors.affiliation: 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.
authors.forename: Ayaz
authors.initials: A
authors.lastname: Ahmad
authors.forename: Xiaofeng
authors.initials: X
authors.lastname: Cao
mesh_terms: D001120:Arginine / Q000378:metabolism*; D018506:Gene Expression Regulation, Plant; D008745:Methylation; D005810:Multigene Family; D063245:Plant Development; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D010944:Plants / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism*
chemical_list: D010940:Plant Proteins; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases