Protein arginine methyltransferase 7 (PRMT7) is a protein that in humans is encoded by the PRMT7 gene. Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PRMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing.
PRMT7 was initially identified as a Type II protein lysine methyltransferase, indicating its role in the symmetric dimethylation of arginine residues. However, it was later reclassified as a Type III protein lysine methyltransferase, meaning it facilitates the mono-methylation of arginine residues. As of 2023, PRMT7 remains the sole member of the Type III PRMT category.
References
- ^ "Protein arginine methyltransferase 7". Retrieved 2011-12-06.
- Miranda, T. B.; Miranda, M.; Frankel, A.; Clarke, S. (2004). "PRMT7 is a Member of the Protein Arginine Methyltransferase Family with a Distinct Substrate Specificity". Journal of Biological Chemistry. 279 (22): 22902–22907. doi:10.1074/jbc.M312904200. PMID 15044439.
- Tollefsbol, Trygve O., ed. (2023). Handbook of epigenetics: the new molecular and medical genetics (Third ed.). London, United Kingdom; San Diego, CA: Academic Press, an imprint of Elseiver. p. 36. ISBN 978-0-323-91909-8.
Further reading
- Jelinic, P.; Stehle, J. C.; Shaw, P. (2006). "The Testis-Specific Factor CTCFL Cooperates with the Protein Methyltransferase PRMT7 in H19 Imprinting Control Region Methylation". PLOS Biology. 4 (11): e355. doi:10.1371/journal.pbio.0040355. PMC 1609128. PMID 17048991.
- Lee, J. -H.; Cook, J. R.; Yang, Z. H.; Mirochnitchenko, O.; Gunderson, S. I.; Felix, A. M.; Herth, N.; Hoffmann, R.; Pestka, S. (2004). "PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine". Journal of Biological Chemistry. 280 (5): 3656–3664. doi:10.1074/jbc.M405295200. PMID 15494416.
- Gonsalvez, G. B.; Tian, L.; Ospina, J. K.; Boisvert, F. -M.; Lamond, A. I.; Matera, A. G. (2007). "Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins". The Journal of Cell Biology. 178 (5): 733–740. doi:10.1083/jcb.200702147. PMC 2064538. PMID 17709427.
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