Protein arginine N-methyltransferase 8

Definition

S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer. Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS.

References:

[1]. Sachiko Toma-Fukai, et al. Novel helical assembly in arginine methyltransferase 8. J Mol Biol. 2016 Mar 27;428(6):1197-1208. [Content Brief]

[2]. Wei-Chao Lee, et al. Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity. Biochemistry. 2015 Dec 29;54(51):7514-23. [Content Brief]

[3]. Joyce Sayegh, et al. Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain. J Biol Chem. 2007 Dec 14;282(50):36444-53. [Content Brief]

[4]. Jaeho Lee, et al. PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J Biol Chem. 2005 Sep 23;280(38):32890-6. [Content Brief]

[5]. Steffen Pahlich, et al. Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state. Proteins. 2008 Sep;72(4):1125-37. [Content Brief]

生物医学辞典

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