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

ABSTRACT: 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.

SUBMITTER: King EA

PROVIDER: S-EPMC8398576 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature

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

King Elizabeth A EA Peairs Emily M EM Uthappa Diya M DM Villa Jordan K JK Goff Cameron M CM Burrow Naya K NK Deitch Rebecca T RT Martin Anna K AK Young Douglas D DD

Molecules (Basel, Switzerland) 20210821 16

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 nitroben ...[more]

PMID: 34443661

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