PRMT1

From Wikipedia, the free encyclopedia

Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Protein arginine N-methyltransferase 1 is an enzyme that in humans is encoded by the PRMT1 gene.[1] The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4.[2]

Function

PRMT1 gene encodes for the protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4 in eukaryotic cells.[2] Specifically altering histone H4 in eukaryotes gives it the ability to remodel chromatin acting as a post-translational modifier.[3]

Through regulation of gene expression, arginine methyltransferases control the cell cycle and death of eukaryotic cells.[3]

Reaction pathway

While all PRMT enzymes catalyze the methylation of arginine residues in proteins, PRMT1 is unique in that is catalyzes the formation of asymmetric dimethylarginine as opposed to the PRMT2 that catalyzes the formation of symmetric dimethylarginine.[4] Individual PRMT utilize S-adenosyl-L-methionine (SAM) as the methyl donor and catalyze methyl group transfer to the ω-nitrogen of an arginine residue.[4]

Clinical significance

In humans, these enzymes regulate gene expression and hence are involved in pathogenesis of many human diseases.[5] Using enzyme inhibitors for arginine methyltransferase 1, studies were able to demonstrate the enzyme's potential as an early catalyst of various cancers.[5][4][6]

Interactions

PRMT1 has been shown to interact with:

Page Template:Div col/styles.css has no content.

References

Page Template:Reflist/styles.css has no content.

  1. ^ Page Module:Citation/CS1/styles.css has no content.Scott HS, Antonarakis SE, Lalioti MD, Rossier C, Silver PA, Henry MF (June 1998). "Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)". Genomics. 48 (3): 330–40. doi:10.1006/geno.1997.5190. PMID 9545638.
  2. ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: PRMT1 protein arginine methyltransferase 1".
  3. ^ a b Page Module:Citation/CS1/styles.css has no content.Qian K, Zhen G (2016-01-01). "Chapter 8 - Current Development of Protein Arginine Methyltransferase Inhibitors". In Medina-Franco JL (ed.). Epi-Informatics. Boston: Academic Press. pp. 231–256. doi:10.1016/b978-0-12-802808-7.00008-3. ISBN 978-0-12-802808-7.
  4. ^ a b c Page Module:Citation/CS1/styles.css has no content.Obianyo O, Osborne TC, Thompson PR (September 2008). "Kinetic mechanism of protein arginine methyltransferase 1". Biochemistry. 47 (39): 10420–7. doi:10.1021/bi800904m. PMC 2933744. PMID 18771293.
  5. ^ a b Page Module:Citation/CS1/styles.css has no content.Zeng H, Xu W (2015-01-01). "Chapter 16 - Enzymatic Assays of Histone Methyltransferase Enzymes". In Zheng YG (ed.). Epigenetic Technological Applications. Boston: Academic Press. pp. 333–361. doi:10.1016/b978-0-12-801080-8.00016-8. ISBN 978-0-12-801080-8.
  6. ^ Page Module:Citation/CS1/styles.css has no content.Carbone F, Montecucco F, Xu S, Banach M, Jamialahmadi T, Sahebkar A (August 2020). "Epigenetics in atherosclerosis: key features and therapeutic implications". Expert Opinion on Therapeutic Targets. 24 (8): 719–721. doi:10.1080/14728222.2020.1764535. PMID 32354276.
  7. ^ a b Page Module:Citation/CS1/styles.css has no content.Lin WJ, Gary JD, Yang MC, Clarke S, Herschman HR (June 1996). "The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase". J. Biol. Chem. 271 (25): 15034–44. doi:10.1074/jbc.271.25.15034. PMID 8663146.
  8. ^ a b Page Module:Citation/CS1/styles.css has no content.Berthet C, Guéhenneux F, Revol V, Samarut C, Lukaszewicz A, Dehay C, Dumontet C, Magaud JP, Rouault JP (January 2002). "Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects". Genes Cells. 7 (1): 29–39. doi:10.1046/j.1356-9597.2001.00497.x. PMID 11856371. S2CID 15016952.
  9. ^ Page Module:Citation/CS1/styles.css has no content.Smith WA, Schurter BT, Wong-Staal F, David M (May 2004). "Arginine methylation of RNA helicase a determines its subcellular localization". J. Biol. Chem. 279 (22): 22795–8. doi:10.1074/jbc.C300512200. PMID 15084609.
  10. ^ a b Page Module:Citation/CS1/styles.css has no content.Lee J, Bedford MT (March 2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Rep. 3 (3): 268–73. doi:10.1093/embo-reports/kvf052. PMC 1084016. PMID 11850402.
  11. ^ a b c Page Module:Citation/CS1/styles.css has no content.Wada K, Inoue K, Hagiwara M (August 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy". Biochim. Biophys. Acta. 1591 (1–3): 1–10. doi:10.1016/s0167-4889(02)00202-1. PMID 12183049.
  12. ^ a b Page Module:Citation/CS1/styles.css has no content.Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  13. ^ a b Page Module:Citation/CS1/styles.css has no content.Côté J, Boisvert FM, Boulanger MC, Bedford MT, Richard S (January 2003). "Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1". Mol. Biol. Cell. 14 (1): 274–87. doi:10.1091/mbc.E02-08-0484. PMC 140244. PMID 12529443.
  14. ^ Page Module:Citation/CS1/styles.css has no content.Abramovich C, Yakobson B, Chebath J, Revel M (January 1997). "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor". EMBO J. 16 (2): 260–6. doi:10.1093/emboj/16.2.260. PMC 1169633. PMID 9029147.
  15. ^ Page Module:Citation/CS1/styles.css has no content.Tang J, Kao PN, Herschman HR (June 2000). "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3". J. Biol. Chem. 275 (26): 19866–76. doi:10.1074/jbc.M000023200. PMID 10749851.
  16. ^ Page Module:Citation/CS1/styles.css has no content.Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB (April 2003). "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties". Mol. Cell. 11 (4): 1055–66. doi:10.1016/s1097-2765(03)00101-1. PMID 12718890.

Further reading

Page Template:Refbegin/styles.css has no content.

Lua error in package.lua at line 80: module 'Module:Navbox/configuration' not found.

Retrieved from "https://cosmopedia.co/index.php?title=PRMT1&oldid=4742814"