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Protein Arginine Methyltransferase 1: Positively Charged Residues In Substrate Peptides Distal To The Site Of Methylation Are Important For Substrate Binding And Catalysis, Tanesha C. Osborne, Obiamaka Obianyo, Xing Zhang, Xiadong Cheng, Paul R. Thompson
Protein Arginine Methyltransferase 1: Positively Charged Residues In Substrate Peptides Distal To The Site Of Methylation Are Important For Substrate Binding And Catalysis, Tanesha C. Osborne, Obiamaka Obianyo, Xing Zhang, Xiadong Cheng, Paul R. Thompson
Tanesha C. Osborne
Protein arginine methyltransferases (PRMTs) are a group of eukaryotic enzymes that catalyze the methylation of Arg residues in a variety of proteins (e.g., histones H3 and H4), and their activities influence a wide range of cellular processes, including cell growth, RNA splicing, differentiation, and transcriptional regulation. Dysregulation of these enzymes has been linked to heart disease and cancer, suggesting this enzyme family as a novel therapeutic target. To aid the development of PRMT inhibitors, we characterized the substrate specificity of both the rat and human PRMT1 orthologues using histone based peptide substrates. N- and C-terminal truncations to identify a minimal …