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 re...

Full description

Saved in:
Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2021-08, Vol.26 (16), p.5072
Main Authors: King, Elizabeth A., Peairs, Emily M., Uthappa, Diya M., Villa, Jordan K., Goff, Cameron M., Burrow, Naya K., Deitch, Rebecca T., Martin, Anna K., Young, Douglas D.
Format: Article
Language:English
Subjects:
Amino acids
Communication
DNA methylation
E coli
Enzymes
Epigenetics
Gene expression
Genomes
Homocysteine
Irradiation
Kinases
Methyltransferase
non-canonical amino acid
Phosphorylation
photoactivation
protein methylation
Proteins
Tyrosine
Ultraviolet radiation
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules26165072