Photoregulation of PRMT-1 Using a Photolabile Non-Canonical Amino Acid

Protein methyltransferases are vital to the epigenetic modification of gene expression. Thus, obtaining a better understanding of and control over the regulation of these crucial proteins has significant implications for the study and treatment of numerous diseases. One ideal mechanism of protein regulation is the specific installation of a photolabile-protecting group through the use of photocaged non-canonical amino acids. Consequently, PRMT1 was caged at a key tyrosine residue with a nitrobenzyl-protected Schultz amino acid to modulate protein function. Subsequent irradiation with UV light removes the caging group and restores normal methyltransferase activity, facilitating the spatial and temporal control of PRMT1 activity. Ultimately, this caged PRMT1 affords the ability to better understand the protein's mechanism of action and potentially regulate the epigenetic impacts of this vital protein.

Automated summary

Protein methyltransferases play a vital role in the epigenetic modification of gene expression, making understanding and controlling their regulation significant for the study and treatment of numerous diseases. By cageing PRMT1 at a specific residue and restoring its activity with UV light, spatial and temporal control of the protein's activity can be achieved, leading to a better understanding of its mechanism of action and potential regulation of its epigenetic impacts.