| Histone-lysine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.43 | ||||||||
| CAS no. | 9055-08-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Histone methyltransferases (HMT) are histone-modifying enzymes (e.g., histone-lysine N-methyltransferases and histone-arginine N-methyltransferases), that catalyze the transfer of one, two, or three methyl groups to lysine and arginine residues of histone proteins. The attachment of methyl groups occurs predominantly at specific lysine or arginine residues on histones H3 and H4.[1] Two major types of histone methyltranferases exist, lysine-specific (which can be SET (Su(var)3-9, Enhancer of Zeste, Trithorax) domain containing or non-SET domain containing) and arginine-specific.[2][3][4] In both types of histone methyltransferases, S-Adenosyl methionine (SAM) serves as a cofactor and methyl donor group.[1][5][6][7]
The genomic DNA of eukaryotes associates with histones to form chromatin.[8] The level of chromatin compaction depends heavily on histone methylation and other post-translational modifications of histones.[9] Histone methylation is a principal epigenetic modification of chromatin[9] that determines gene expression, genomic stability, stem cell maturation, cell lineage development, genetic imprinting, DNA methylation, and cell mitosis.[2]
- ^ a b Wood A, Shilatifard A (2004). "Posttranslational Modifications of Histones by Methylation". In Conaway JW, Conaway RC (eds.). Proteins in eukaryotic transcription. Advances in Protein Chemistry. Vol. 67. Amsterdam: Elsevier Academic Press. pp. 201–222. doi:10.1016/S0065-3233(04)67008-2. ISBN 0-12-034267-7. PMID 14969729.
- ^ a b Sawan C, Herceg Z (2010). "Histone Modifications and Cancer". In Ushijima T, Herceg Z (eds.). Epigenetics and Cancer, Part A, Volume 70. Advances in Genetics. Vol. 70. Boston: Academic Press. pp. 57–85. doi:10.1016/B978-0-12-380866-0.60003-4. ISBN 978-0-12-380866-0. PMID 20920745.
- ^ Feng Q, Wang H, Ng HH, Erdjument-Bromage H, Tempst P, Struhl K, Zhang Y (June 2002). "Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain". Curr. Biol. 12 (12): 1052–8. doi:10.1016/S0960-9822(02)00901-6. PMID 12123582. S2CID 17263035.
- ^ Ng HH, Feng Q, Wang H, Erdjument-Bromage H, Tempst P, Zhang Y, Struhl K (June 2002). "Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association". Genes Dev. 16 (12): 1518–27. doi:10.1101/gad.1001502. PMC 186335. PMID 12080090.
- ^ Branscombe TL, Frankel A, Lee JH, Cook JR, Yang Z, Pestka S, Clarke S (August 2001). "PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins". J. Biol. Chem. 276 (35): 32971–6. doi:10.1074/jbc.M105412200. PMID 11413150.
- ^ Weiss VH, McBride AE, Soriano MA, Filman DJ, Silver PA, Hogle JM (December 2000). "The structure and oligomerization of the yeast arginine methyltransferase, Hmt1". Nat. Struct. Biol. 7 (12): 1165–71. doi:10.1038/82028. PMID 11101900. S2CID 11575783.
- ^ Zhang X, Zhou L, Cheng X (July 2000). "Crystal structure of the conserved core of protein arginine methyltransferase PRMT3". EMBO J. 19 (14): 3509–19. doi:10.1093/emboj/19.14.3509. PMC 313989. PMID 10899106.
- ^ "Chromatin Network". Retrieved 1 March 2012.
- ^ a b Kouzarides T (February 2007). "Chromatin modifications and their function". Cell. 128 (4): 693–705. doi:10.1016/j.cell.2007.02.005. PMID 17320507.