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


Journal

Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009

Informations de publication

Date de publication:
21 Aug 2021
Historique:
received: 15 07 2021
revised: 10 08 2021
accepted: 11 08 2021
entrez: 27 8 2021
pubmed: 28 8 2021
medline: 1 10 2021
Statut: epublish

Résumé

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.

Identifiants

pubmed: 34443661
pii: molecules26165072
doi: 10.3390/molecules26165072
pmc: PMC8398576
pii:
doi:

Substances chimiques

Amino Acids 0
Repressor Proteins 0
Transcription Factors 0
Tyrosine 42HK56048U
Protein Methyltransferases EC 2.1.1.-
PRMT1 protein, human EC 2.1.1.319
Protein-Arginine N-Methyltransferases EC 2.1.1.319

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : R15 GM113203
Pays : United States
Organisme : NIH HHS
ID : R15GM113203
Pays : United States

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Auteurs

Elizabeth A King (EA)

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

Emily M Peairs (EM)

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

Diya M Uthappa (DM)

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

Jordan K Villa (JK)

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

Cameron M Goff (CM)

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

Naya K Burrow (NK)

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

Rebecca T Deitch (RT)

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

Anna K Martin (AK)

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

Douglas D Young (DD)

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

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Classifications MeSH