The current thrust in our laboratory are investigations centered on a family of human enzymes called protein arginine N-methyltransferases (PRMTs), which transfer methyl groups from S-adenosyl-L-methionine to arginine residues within proteins. Chemically, this post-translational modification alte...
The current thrust in our laboratory are investigations centered on a family of human enzymes called protein arginine N-methyltransferases (PRMTs), which transfer methyl groups from S-adenosyl-L-methionine to arginine residues within proteins. Chemically, this post-translational modification alters the hydrogen-bonding capability of the decorated residue without significantly changing its positive charge. Biologically, arginine methylation plays important roles in facilitating gene expression and repression, processing nascent RNA transcripts, and participating in DNA damage repair. To learn more about ongoing projects in the laboratory, please contact Dr. Frankel directly.