PRMT7

PRMT7, or protein arginine methyltransferase 7, is an enzyme in the PRMT family that modifies arginine residues on substrate proteins through methylation. It is classified as a type III PRMT, which predominantly catalyzes the formation of monomethylarginine (MMA) rather than dimethylated products.

The catalytic activity of PRMT7 uses S-adenosyl-L-methionine (SAM) as the methyl donor. PRMT7 generally functions as a homodimer and requires proper protein conformation for activity. Its substrate range includes histone and non-histone proteins, contributing to regulation of chromatin structure, gene expression, RNA processing, and signaling pathways. Evidence from cell-based and model organism studies indicates that PRMT7 influences development, stress responses, and germ cell biology.

PRMT7 localizes to both the cytoplasm and nucleus, and its activity can be modulated by interacting partners and cellular context. The enzyme is conserved across metazoans, reflecting its broad role in post-translational modification.

Dysregulation of PRMT7 has been associated with human diseases, including cancer and immune or neurological disorders, making it a focus of research as a potential therapeutic target. In addition, PRMT7 inhibitors and chemical probes are used in preclinical studies to dissect function and assess therapeutic potential.