Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)

Abstract

Sequencing of the PRMT3 gene in patients from the Czech DBA registry revealed a heterozygous mutation encoding the Tyr87Cys substitution. To address the impact of the mutation and putative Tyr87 phosphorylation on PRMT3 properties, we constructed two additional PRMT3 variants, Tyr87Phe and Tyr87Glu PRMT3, mimicking non-phosphorylated and phosphorylated Tyr87, respectively and studied their activity.

In conclusion, Tyr87 is important for the interaction between PRMT3 and RPS2 and for its full enzymatic activity

Keywords

• PRMT3
• RPS2
• arginine methylation