| 货号 | 13563S |
| 供应商 | CST |
| 背景 | Arginine methylation is a prevalent PTM found on both nuclear and cytoplasmic proteins. Arginine methylated proteins are involved in many different cellular processes, including transcriptional regulation, signal transduction, RNA metabolism, and DNA damage repair (1-3). Arginine methylation is carried out by the arginine N-methyltransferase (PRMT) family of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (4). There are three different types of arginine methylation: asymmetric dimethylarginine (aDMA, omega-NG,NG-dimethylarginine), where two methyl groups are placed on one of the terminal nitrogen atoms of the guanidine group of arginine; symmetric dimethylarginine (sDMA, omega-NG,N’G-dimethylarginine), where one methyl group is placed on each of the two terminal guanidine nitrogens of arginine; and monomethylarginine (MMA, omega-NG-dimethylarginine), where a single methyl group is placed on one of the terminal nitrogen atoms of arginine. Each of these modifications has potentially different functional consequences. Though all PRMT proteins catalyze the formation of MMA, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce aDMA, while Type II PRMTs (PRMT5 and 7) produce sDMA. Methylated arginine residues often reside in glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (5). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within proline-glycine-methionine rich (PGM) motifs (6). |
| 存放说明 | -20C |
| 参考文献 | Bedford, M.T. and Richard, S. (2005) Mol Cell 18, 263-72. Pahlich, S. et al. (2006) Biochim Biophys Acta 1764, 1890-903. Bedford, M.T. and Clarke, S.G. (2009) Mol Cell 33, 1-13. McBride, A.E. and Silver, P.A. (2001) Cell 106, 5-8. Gary, J.D. and Clarke, S. (1998) Prog Nucleic Acid Res Mol Biol 61, 65-131. Cheng, D. et al. (2007) Mol Cell 25, 71-83. Chittka, A. (2010) PLoS One 5, e13807. |
The Motif Logo was generated from a MethylScan® LC-MS/MS experiment using 95 nonredundant tryptic peptides derived from mouse embryo immunoprecipitated with PTMScan® Symmetric Di-Methyl Arginine Motif [sdme-RG] Immunoaffinity Beads. The logo represents the relative frequency of amino acids in each position surrounding the central symmetrically di-methylated arginine residue. Glycine residues are enriched, especially at the +1 and -1 positions, in the context of symmetric di-methyl arginine when compared to the overall expected frequency in the mouse proteome. | |
This chart shows the relative category distribution of proteins with symmetrically di-methylated arginine identified from peptides generated from a MethylScan® LC-MS/MS experiment of mouse embryo using PTMScan® Symmetric Di-Methyl Arginine Motif [sdme-RG] Immunoaffinity Beads. |
