Protein Arginine Methyltransferase 1 (PRMT1) is a member of the protein arginine methyltransferase family, which plays a crucial role in the post-translational modification of proteins. PRMT1 is the predominant arginine methyltransferase in mammals, responsible for more than 85% of the arginine methylation activity in cells . This enzyme is involved in various cellular processes, including transcriptional regulation, RNA processing, DNA repair, and signal transduction .
PRMT1 catalyzes the transfer of methyl groups from S-adenosylmethionine (AdoMet) to the guanidine nitrogen atoms of arginine residues in target proteins, forming monomethylarginine and asymmetric dimethylarginine . This methylation process increases the structural diversity of proteins and modulates their function within the cell .
PRMT1 is a type-I methyltransferase that specifically targets histone H4 in eukaryotic cells, altering its structure and enabling chromatin remodeling . This modification is essential for the regulation of gene expression and maintenance of genomic integrity .
PRMT1 is critical for various biological processes, including:
In mouse models, PRMT1 has been shown to regulate various physiological processes. For instance, PRMT1 is essential for the development and homeostasis of enteroendocrine cells in the adult intestinal epithelium . Enteroendocrine cells are hormone-producing cells that play a crucial role in energy homeostasis and metabolism . PRMT1 deficiency in mice leads to an increase in the number of enteroendocrine cells and upregulation of enteroendocrine-specific hormones and transcription factors .