Protein arginine N-methyltransferase 7

Definition:

Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.

References:

[1]. Jin-Hyung Lee, et al. PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine. J Biol Chem. 2005 Feb 4;280(5):3656-64. [Content Brief]

[2]. Graydon B Gonsalvez, et al. Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J Cell Biol. 2007 Aug 27;178(5):733-40. [Content Brief]

[3]. Tina Branscombe Miranda, et al. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J Biol Chem. 2004 May 28;279(22):22902-7. [Content Brief]

[4]. Hao Wang, et al. Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry. J Am Soc Mass Spectrom. 2009 Mar;20(3):507-19. [Content Brief]

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