PRMT1

PRMT1 gene encodes for the protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4 in eukaryotic cells.{{cite web | title = Entrez Gene: PRMT1 protein arginine methyltransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3276}} Specifically altering histone H4 in eukaryotes gives it the ability to remodel chromatin acting as a post-translational modifier.

Through regulation of gene expression, arginine methyltransferases control the cell cycle and death of eukaryotic cells.{{cite book | vauthors = Qian K, Zhen G | chapter = Chapter 8 - Current Development of Protein Arginine Methyltransferase Inhibitors|date=2016-01-01 | title = Epi-Informatics|pages=231–256| veditors = Medina-Franco JL |place=Boston|publisher=Academic Press|language=en|doi=10.1016/b978-0-12-802808-7.00008-3|isbn=978-0-12-802808-7 }}

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 symmetrically dimethylated arginine.{{cite journal | vauthors = Obianyo O, Osborne TC, Thompson PR | title = Kinetic mechanism of protein arginine methyltransferase 1 | journal = Biochemistry | volume = 47 | issue = 39 | pages = 10420–7 | date = September 2008 | pmid = 18771293 | pmc = 2933744 | doi = 10.1021/bi800904m }} 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.

In humans, these enzymes regulate gene expression and hence are involved in pathogenesis of many human diseases.{{cite book | vauthors = Zeng H, Xu W |chapter=Chapter 16 - Enzymatic Assays of Histone Methyltransferase Enzymes|date=2015-01-01 | title = Epigenetic Technological Applications|pages=333–361| veditors = Zheng YG |place=Boston|publisher=Academic Press |doi=10.1016/b978-0-12-801080-8.00016-8|isbn=978-0-12-801080-8 }} Using enzyme inhibitors for arginine methyltransferase 1, studies were able to demonstrate the enzyme's potential as an early catalyst of various cancers.{{cite journal | vauthors = Carbone F, Montecucco F, Xu S, Banach M, Jamialahmadi T, Sahebkar A | title = Epigenetics in atherosclerosis: key features and therapeutic implications | journal = Expert Opinion on Therapeutic Targets | volume = 24 | issue = 8 | pages = 719–721 | date = August 2020 | pmid = 32354276 | doi = 10.1080/14728222.2020.1764535 | doi-access = free }}

PRMT1 has been shown to interact with:

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• BTG1,
• BTG2,{{cite journal | vauthors = Lin WJ, Gary JD, Yang MC, Clarke S, Herschman HR | title = The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase | journal = J. Biol. Chem. | volume = 271 | issue = 25 | pages = 15034–44 | date = June 1996 | pmid = 8663146 | doi = 10.1074/jbc.271.25.15034| doi-access = free }}{{cite journal | vauthors = Berthet C, Guéhenneux F, Revol V, Samarut C, Lukaszewicz A, Dehay C, Dumontet C, Magaud JP, Rouault JP | title = Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects | journal = Genes Cells | volume = 7 | issue = 1 | pages = 29–39 | date = January 2002 | pmid = 11856371 | doi = 10.1046/j.1356-9597.2001.00497.x | s2cid = 15016952 | doi-access = free }}
• DHX9,{{cite journal | vauthors = Smith WA, Schurter BT, Wong-Staal F, David M | title = Arginine methylation of RNA helicase a determines its subcellular localization | journal = J. Biol. Chem. | volume = 279 | issue = 22 | pages = 22795–8 | date = May 2004 | pmid = 15084609 | doi = 10.1074/jbc.C300512200 | doi-access = free }}
• FUS,
• HNRNPR,{{cite journal | vauthors = 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 | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | date = September 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 | hdl = 11858/00-001M-0000-0010-8592-0 | s2cid = 8235923 | hdl-access = free }}
• HNRPK,{{cite journal | vauthors = Wada K, Inoue K, Hagiwara M | title = Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy | journal = Biochim. Biophys. Acta | volume = 1591 | issue = 1–3 | pages = 1–10 | date = August 2002 | pmid = 12183049 | doi = 10.1016/s0167-4889(02)00202-1 | doi-access = free }}
• IFNAR1,{{cite journal | vauthors = Abramovich C, Yakobson B, Chebath J, Revel M | title = A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor | journal = EMBO J. | volume = 16 | issue = 2 | pages = 260–6 | date = January 1997 | pmid = 9029147 | pmc = 1169633 | doi = 10.1093/emboj/16.2.260 }}
• ILF3,{{cite journal | vauthors = Lee J, Bedford MT | title = PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays | journal = EMBO Rep. | volume = 3 | issue = 3 | pages = 268–73 | date = March 2002 | pmid = 11850402 | pmc = 1084016 | doi = 10.1093/embo-reports/kvf052 }}{{cite journal | vauthors = Tang J, Kao PN, Herschman HR | title = Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3 | journal = J. Biol. Chem. | volume = 275 | issue = 26 | pages = 19866–76 | date = June 2000 | pmid = 10749851 | doi = 10.1074/jbc.M000023200 | doi-access = free }}
• KHDRBS1,{{cite journal | vauthors = Côté J, Boisvert FM, Boulanger MC, Bedford MT, Richard S | title = Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1 | journal = Mol. Biol. Cell | volume = 14 | issue = 1 | pages = 274–87 | date = January 2003 | pmid = 12529443 | pmc = 140244 | doi = 10.1091/mbc.E02-08-0484 }} and
• SUPT5H.{{cite journal |author8-link=Richard Gaynor| vauthors = Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB | title = Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties | journal = Mol. Cell | volume = 11 | issue = 4 | pages = 1055–66 | date = April 2003 | pmid = 12718890 | doi = 10.1016/s1097-2765(03)00101-1 | doi-access = free }}

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{{reflist|30em}}

{{refbegin|30em}}

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• {{cite journal | vauthors = Klein S, Carroll JA, Chen Y, Henry MF, Henry PA, Ortonowski IE, Pintucci G, Beavis RC, Burgess WH, Rifkin DB | title = Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2 | journal = J. Biol. Chem. | volume = 275 | issue = 5 | pages = 3150–7 | year = 2000 | pmid = 10652299 | doi = 10.1074/jbc.275.5.3150 | doi-access = free }}
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• {{cite journal | vauthors = Mowen KA, Tang J, Zhu W, Schurter BT, Shuai K, Herschman HR, David M | title = Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription | journal = Cell | volume = 104 | issue = 5 | pages = 731–41 | year = 2001 | pmid = 11257227 | doi = 10.1016/S0092-8674(01)00269-0 | s2cid = 17584895 | doi-access = free }}
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• {{cite journal | vauthors = Strahl BD, Briggs SD, Brame CJ, Caldwell JA, Koh SS, Ma H, Cook RG, Shabanowitz J, Hunt DF, Stallcup MR, Allis CD | title = Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1 | journal = Curr. Biol. | volume = 11 | issue = 12 | pages = 996–1000 | year = 2001 | pmid = 11448779 | doi = 10.1016/S0960-9822(01)00294-9 | s2cid = 17783289 | doi-access = free | bibcode = 2001CBio...11..996S }}
• {{cite journal | vauthors = Rho J, Choi S, Seong YR, Choi J, Im DS | title = The Arginine-1493 Residue in QRRGRTGR1493G Motif IV of the Hepatitis C Virus NS3 Helicase Domain Is Essential for NS3 Protein Methylation by the Protein Arginine Methyltransferase 1 | journal = J. Virol. | volume = 75 | issue = 17 | pages = 8031–44 | year = 2001 | pmid = 11483748 | pmc = 115047 | doi = 10.1128/JVI.75.17.8031-8044.2001 }}
• {{cite journal | vauthors = Lee J, Bedford MT | title = PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays | journal = EMBO Rep. | volume = 3 | issue = 3 | pages = 268–73 | year = 2002 | pmid = 11850402 | pmc = 1084016 | doi = 10.1093/embo-reports/kvf052 }}

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• {{PDBe-KB2|Q99873|Protein arginine N-methyltransferase 1}}

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Category:Genes mutated in mice