Characterization of the Activity and Biological Function of Human Protein Arginine Methyltransferase 9 (PRMT9)

• DOI: 10.1096/fasebj.29.1_supplement.lb211
• Publication Date: 2021-06-21T19:10:26Z
• Authors: Andrea Hadjikyriacou; Yanzhong Yang; Mark Bedford; Steven Clarke
• Keywords: Protein methylation; Transferase

Protein arginine methyltransferases (PRMTs) make up a family of enzymes that transfer methyl groups onto residues and play important roles in DNA repair, splicing, transcriptional control signaling. In mammals, nine PRMTs are known. PRMT1,2,3,4,6, 8 catalyze the formation asymmetric dimethylarginine (ADMA) w‐monomethylarginine (MMA), PRMT5 catalyzes symmetric (SDMA) MMA formation, PRMT7 only formation. The last member this family, PRMT9 (also designated PRMT10), has not previously been characterized. humans, it is encoded on gene chromosome 4 position 4q31. We have now expressed human both as GST‐fusion protein bacterial cells GFP‐fusion HEK293 cells. For expression systems, we also prepared catalytic mutants to serve controls for possible contamination other types PRMTs. Using an vitro methylation assay, show forms myelin basic N‐terminal domain fibrillarin. Studies progress characterize type activity physiological substrates PRMT9.