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

Molecules

Douglas D. Young¹  Elizabeth A. King¹  Naya K. Burrow¹  Rebecca T. Deitch¹  Anna K. Martin¹  Emily M. Peairs¹  Cameron M. Goff¹  Diya M. Uthappa¹  Jordan K. Villa¹ 

[1] Department of Chemistry, College of William & Mary, P.O. Box 8795, Williamsburg, VA 23187, USA;

关键词: non-canonical amino acid;    photoactivation;    protein methylation;   

DOI  :  10.3390/molecules26165072

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown