Protein arginine methyltransferase 5
Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene.[1][2]
Model organisms
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Abnormal |
| Recessive lethal study | Abnormal |
| Fertility | Normal |
| 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 | Normal |
| Plasma immunoglobulins | Normal |
| Haematology | Normal[3] |
| Peripheral blood lymphocytes | Normal |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Brain histopathology | Normal |
| Salmonella infection | Normal[4] |
| Citrobacter infection | Normal[5] |
| All tests and analysis from[6][7] |
Model organisms have been used in the study of PRMT5 function. A conditional knockout mouse line, called Prmt5tm2a(EUCOMM)Wtsi[8][9] 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.[10][11][12]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[6][13] Twenty five tests were carried out on mutant mice and two significant abnormalities were observed.[6] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice but no further abnormalities were observed.[6]
Interactions
Protein arginine methyltransferase 5 has been shown to interact with:
- CLNS1A,[14][15][16]
- Janus kinase 2,[17]
- SNRPD3,[16]
- SUPT5H,[18] and
- WD repeat-containing protein 77.[14]
References
- ↑ Gilbreth M, Yang P, Bartholomeusz G, Pimental RA, Kansra S, Gadiraju R et al. (Jan 1999). "Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs". Proc Natl Acad Sci U S A 95 (25): 14781–6. doi:10.1073/pnas.95.25.14781. PMC 24526. PMID 9843966.
- ↑ "Entrez Gene: PRMT5 protein arginine methyltransferase 5".
- ↑ "Haematology data for Prmt5". Wellcome Trust Sanger Institute.
- ↑ "Salmonella infection data for Prmt5". Wellcome Trust Sanger Institute.
- ↑ "Citrobacter infection data for Prmt5". Wellcome Trust Sanger Institute.
- ↑ 6.0 6.1 6.2 6.3 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.
- ↑ 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 et al. (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.
- ↑ 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.
- ↑ 14.0 14.1 Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M et al. (Mar 2002). "A novel WD repeat protein component of the methylosome binds Sm proteins". J. Biol. Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200. PMID 11756452.
- ↑ Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE (May 1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology". J. Biol. Chem. 273 (18): 10811–4. doi:10.1074/jbc.273.18.10811. PMID 9556550.
- ↑ 16.0 16.1 Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G et al. (Dec 2001). "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins". Mol. Cell. Biol. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994. PMID 11713266.
- ↑ Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S (Oct 1999). "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity". J. Biol. Chem. 274 (44): 31531–42. doi:10.1074/jbc.274.44.31531. PMID 10531356.
- ↑ Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B et al. (Apr 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
- Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE (1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology.". J. Biol. Chem. 273 (18): 10811–4. doi:10.1074/jbc.273.18.10811. PMID 9556550.
- Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S (1999). "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity.". J. Biol. Chem. 274 (44): 31531–42. doi:10.1074/jbc.274.44.31531. PMID 10531356.
- Schwärzler A, Kreienkamp HJ, Richter D (2000). "Interaction of the somatostatin receptor subtype 1 with the human homolog of the Shk1 kinase-binding protein from yeast.". J. Biol. Chem. 275 (13): 9557–62. doi:10.1074/jbc.275.13.9557. PMID 10734105. Vancouver style error (help)
- 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.
- Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G et al. (2001). "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins.". Mol. Cell. Biol. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994. PMID 11713266.
- Brahms H, Meheus L, de Brabandere V, Fischer U, Lührmann R (2001). "Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.". RNA 7 (11): 1531–42. doi:10.1017/S135583820101442X. PMC 1370196. PMID 11720283. Vancouver style error (help)
- Meister G, Eggert C, Bühler D, Brahms H, Kambach C, Fischer U (2002). "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln.". Curr. Biol. 11 (24): 1990–4. doi:10.1016/S0960-9822(01)00592-9. PMID 11747828. Vancouver style error (help)
- Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M et al. (2002). "A novel WD repeat protein component of the methylosome binds Sm proteins.". J. Biol. Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200. PMID 11756452.
- Fabbrizio E, El Messaoudi S, Polanowska J, Paul C, Cook JR, Lee JH et al. (2003). "Negative regulation of transcription by the type II arginine methyltransferase PRMT5.". EMBO Rep. 3 (7): 641–5. doi:10.1093/embo-reports/kvf136. PMC 1084190. PMID 12101096.
- Jiang LQ, Wen SJ, Wang HY, Chen LY (2003). "Screening the proteins that interact with calpain in a human heart cDNA library using a yeast two-hybrid system.". Hypertens. Res. 25 (4): 647–52. doi:10.1291/hypres.25.647. PMID 12358155.
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
- Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B et al. (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.
- Pal S, Yun R, Datta A, Lacomis L, Erdjument-Bromage H, Kumar J et al. (2003). "mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad.". Mol. Cell. Biol. 23 (21): 7475–87. doi:10.1128/MCB.23.21.7475-7487.2003. PMC 207647. PMID 14559996.
- Yanagida M, Hayano T, Yamauchi Y, Shinkawa T, Natsume T, Isobe T et al. (2004). "Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexes.". J. Biol. Chem. 279 (3): 1607–14. doi:10.1074/jbc.M305604200. PMID 14583623.
- Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
- Miranda TB, Khusial P, Cook JR, Lee JH, Gunderson SI, Pestka S et al. (2004). "Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus.". Biochem. Biophys. Res. Commun. 323 (2): 382–7. doi:10.1016/j.bbrc.2004.08.107. PMID 15369763.
- Pal S, Vishwanath SN, Erdjument-Bromage H, Tempst P, Sif S (2004). "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes.". Mol. Cell. Biol. 24 (21): 9630–45. doi:10.1128/MCB.24.21.9630-9645.2004. PMC 522266. PMID 15485929.