PRMT1
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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[edit]
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[edit]
While all PRMT enzymes catalyze the methylation of arginine residues in proteins, PRMT1 is unique in that is catalyzes the formation of asymmetrically dimethylated arginine as opposed to the PRMT2 that catalyzes the formation of symmetrically dimethylated arginine.[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[edit]
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[edit]
PRMT1 has been shown to interact with:
Model organisms[edit]
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Abnormal |
| Recessive lethal study | Abnormal |
| Body weight | Normal |
| Anxiety | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Abnormal[17] |
| Plasma immunoglobulins | Normal |
| Haematology | Normal |
| Peripheral blood lymphocytes | Normal |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Skin Histopathology | Normal |
| Brain histopathology | Normal |
| All tests and analysis from[18][19] |
Model organisms have been used to study PRMT1 function and structure.
A conditional knockout mouse line, called Prmt1tm1a(EUCOMM)Wtsi[20][21] was generated as part of the International Knockout Mouse Consortium program—a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[22][23][24]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[18][25] Twenty three tests were carried out on mutant mice and three significant abnormalities were observed.[18] No homozygous mutant embryos were identified during gestation, and thus none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and females displayed increased circulating creatinine levels.[18]
References[edit]
- ^ 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.
- ^ a b "Entrez Gene: PRMT1 protein arginine methyltransferase 1".
- ^ a b 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.
- ^ a b c 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.
- ^ a b 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.
- ^ 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.
- ^ a b 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.
- ^ a b 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.
- ^ 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.
- ^ a b 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.
- ^ a b c 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.
- ^ a b 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.
- ^ a b 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ "Clinical chemistry data for Prmt1". Wellcome Trust Sanger Institute.
- ^ a b c d Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
- ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ^ "International Knockout Mouse Consortium".
- ^ "Mouse Genome Informatics".
- ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ^ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
- ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
Further reading[edit]
- Kim S, Park GH, Paik WK (1999). "Recent advances in protein methylation: enzymatic methylation of nucleic acid binding proteins". Amino Acids. 15 (4): 291–306. doi:10.1007/BF01320895. PMID 9891755. S2CID 28412209.
- Baldwin GS, Carnegie PR (1971). "Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin". Science. 171 (3971): 579–81. Bibcode:1971Sci...171..579B. doi:10.1126/science.171.3971.579. PMID 4924231. S2CID 36959912.
- Rajpurohit R, Lee SO, Park JO, Paik WK, Kim S (1994). "Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase". J. Biol. Chem. 269 (2): 1075–82. doi:10.1016/S0021-9258(17)42223-X. PMID 8288564.
- Lin WJ, Gary JD, Yang MC, Clarke S, Herschman HR (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.
- Nikawa J, Nakano H, Ohi N (1996). "Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant". Gene. 171 (1): 107–11. doi:10.1016/0378-1119(96)00073-X. PMID 8675017.
- Abramovich C, Yakobson B, Chebath J, Revel M (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.
- Klein S, Carroll JA, Chen Y, Henry MF, Henry PA, Ortonowski IE, Pintucci G, Beavis RC, Burgess WH, Rifkin DB (2000). "Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2". J. Biol. Chem. 275 (5): 3150–7. doi:10.1074/jbc.275.5.3150. PMID 10652299.
- Tang J, Kao PN, Herschman HR (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.
- Nichols RC, Wang XW, Tang J, Hamilton BJ, High FA, Herschman HR, Rigby WF (2000). "The RGG domain in hnRNP A2 affects subcellular localization". Exp. Cell Res. 256 (2): 522–32. doi:10.1006/excr.2000.4827. PMID 10772824.
- Zhang X, Zhou L, Cheng X (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.
- Koh SS, Chen D, Lee YH, Stallcup MR (2001). "Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities". J. Biol. Chem. 276 (2): 1089–98. doi:10.1074/jbc.M004228200. PMID 11050077.
- Scorilas A, Black MH, Talieri M, Diamandis EP (2001). "Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene". Biochem. Biophys. Res. Commun. 278 (2): 349–59. doi:10.1006/bbrc.2000.3807. PMID 11097842.
- Rho J, Choi S, Seong YR, Cho WK, Kim SH, Im DS (2001). "Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family". J. Biol. Chem. 276 (14): 11393–401. doi:10.1074/jbc.M008660200. PMID 11152681.
- Mowen KA, Tang J, Zhu W, Schurter BT, Shuai K, Herschman HR, David M (2001). "Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription". Cell. 104 (5): 731–41. doi:10.1016/S0092-8674(01)00269-0. PMID 11257227. S2CID 17584895.
- Wang H, Huang ZQ, Xia L, Feng Q, Erdjument-Bromage H, Strahl BD, Briggs SD, Allis CD, Wong J, Tempst P, Zhang Y (2001). "Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor". Science. 293 (5531): 853–7. doi:10.1126/science.1060781. PMID 11387442. S2CID 33566292.
- Strahl BD, Briggs SD, Brame CJ, Caldwell JA, Koh SS, Ma H, Cook RG, Shabanowitz J, Hunt DF, Stallcup MR, Allis CD (2001). "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1". Curr. Biol. 11 (12): 996–1000. doi:10.1016/S0960-9822(01)00294-9. PMID 11448779. S2CID 17783289.
- Rho J, Choi S, Seong YR, Choi J, Im DS (2001). "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". J. Virol. 75 (17): 8031–44. doi:10.1128/JVI.75.17.8031-8044.2001. PMC 115047. PMID 11483748.
- Lee J, Bedford MT (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.
External links[edit]
- Overview of all the structural information available in the PDB for UniProt: Q99873 (Protein arginine N-methyltransferase 1) at the PDBe-KB.
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