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Details on Person Arginine methylation is a common post-translational modifica...
| Class:Id | Summation:3215350 |
|---|---|
| _displayName | Arginine methylation is a common post-translational modifica... |
| _timestamp | 2014-07-21 12:33:04 |
| created | [InstanceEdit:3215329] Jupe, S, 2013-03-15 |
| literatureReference | [LiteratureReference:3215360] Distribution of NG, NG,-dimethylarginine in nuclear protein fractions [LiteratureReference:3215328] Protein arginine methylation in mammals: who, what, and why [LiteratureReference:3215374] Protein arginine methyltransferases and cancer [LiteratureReference:3215349] The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing [LiteratureReference:3215145] Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53 [LiteratureReference:3215351] Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes [LiteratureReference:5423564] Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications [LiteratureReference:3215343] Histone H4 acetylation differentially modulates arginine methylation by an in Cis mechanism [LiteratureReference:5205809] Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive [LiteratureReference:5423545] Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation [LiteratureReference:5205806] PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation |
| modified | [InstanceEdit:3215411] Jupe, S, 2013-03-15 [InstanceEdit:5216237] Jupe, S, 2013-12-16 [InstanceEdit:5423532] Jupe, Steve, 2014-05-09 [InstanceEdit:5609983] Jupe, Steve, 2014-07-18 [InstanceEdit:5610084] Jupe, Steve, 2014-07-21 |
| text | Arginine methylation is a common post-translational modification; around 2% of arginine residues are methylated in rat liver nuclei (Boffa et al. 1977). Arginine can be methylated in 3 different ways: monomethylarginine (MMA); NG,NG-asymmetric dimethylarginine (ADMA) and NG,N'G-symmetric dimethylarginine (SDMA). The formation of MMA, ADMA and SDMA in mammalian cells is carried out by members of a family of nine protein arginine methyltransferases (PRMTs) (Bedford & Clarke 2009). Type I, II and III PRMTs generate MMA on one of the two terminal guanidino nitrogen atoms. Subsequent generation of asymmetric dimethylarginine (ADMA) is catalysed by the type I enzymes PRMT1, PRMT2, PRMT3, co-activator-associated arginine methyltransferase 1 (CARM1), PRMT6 and PRMT8. Production of symmetric dimethylarginine (SDMA) is catalysed by the type II enzymes PRMT5 and PRMT7. On certain substrates, PRMT7 also functions as a type III enzyme, generating MMA only. PRMT9 activity has not been characterized. No known enzyme is capable of both ADMA and SDMA modifications. Arginine methylation is regarded as highly stable; no arginine demethylases are known (Yang & Bedford 2013). Most PRMTs methylate glycine- and arginine-rich (GAR) motifs in their substrates (Boffa et al. 1977). CARM1 methylates a proline-, glycine- and methionine-rich (PGM) motif (Cheng et al. 2007). PRMT5 can dimethylate arginine residues in GAR and PGM motifs (Cheng et al. 2007, Branscombe et al. 2001). PRMTs are widely expressed and are constitutively active as purified recombinant proteins. However, PRMT activity can be regulated through PTMs, association with regulatory proteins, subcellular compartmentalization and factors that affect enzyme-substrate interactions. The target sites of PRMTs are influenced by the presence of other PTMs on their substrates. The best characterized examples of this are for histones. Histone H3 lysine-19 acetylation (H3K18ac) primes the histone tail for asymmetric dimethylation at arginine-18 (H3R17me2a) by CARM1 (An et al. 2003, Daujat et al. 2002, Yue et al. 2007). H3 lysine-10 acetylation (H3K9ac) blocks arginine-9 symmetric dimethylation (H3R8me2s) by PRMT5 (Pal et al. 2004). H4R3me2a catalyzed by PRMT1 favours subsequent acetylation of the histone H4 tail (Huang et al. 2005). At the same time histone H4 lysine-5 acetylation (H4K5ac) makes the H4R3 motif a better substrate for PRMT5 compared with PRMT1, thereby moving the balance from an activating ADMA mark to a suppressive SDMA mark at the H4R3 motif (Feng et al. 2011). Finally methylation of Histone H3 on arginine-3 (H3R2me2a) by PRMT6 blocks methylation of H3 lysine-5 by the MLL complex (H3K4me3), and vice versa, methylation of H3K4me3 prevents H3R2me2a methylation (Guccione et al. 2007, Kirmizis et al. 2007, Hyllus et al. 2007). N.B. The coordinates of post-translational modifications represented and described here follow UniProt standard practice whereby coordinates refer to the translated protein before any further processing. Histone literature typically refers to coordinates of the protein after the initiating methionine has been removed. Therefore the coordinates of post-translated residues in the Reactome database and described here are frequently +1 when compared with the literature. |
| (summation) | [Pathway:3214858] RMTs methylate histone arginines [Homo sapiens] |
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