Cargando…

Structure, Activity, and Function of PRMT1

PRMT1, the major protein arginine methyltransferase in mammals, catalyzes monomethylation and asymmetric dimethylation of arginine side chains in proteins. Initially described as a regulator of chromatin dynamics through the methylation of histone H4 at arginine 3 (H4R3), numerous non-histone substr...

Descripción completa

Detalles Bibliográficos
Autores principales: Thiebaut, Charlène, Eve, Louisane, Poulard, Coralie, Le Romancer, Muriel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619983/
https://www.ncbi.nlm.nih.gov/pubmed/34833023
http://dx.doi.org/10.3390/life11111147
_version_ 1784605115579105280
author Thiebaut, Charlène
Eve, Louisane
Poulard, Coralie
Le Romancer, Muriel
author_facet Thiebaut, Charlène
Eve, Louisane
Poulard, Coralie
Le Romancer, Muriel
author_sort Thiebaut, Charlène
collection PubMed
description PRMT1, the major protein arginine methyltransferase in mammals, catalyzes monomethylation and asymmetric dimethylation of arginine side chains in proteins. Initially described as a regulator of chromatin dynamics through the methylation of histone H4 at arginine 3 (H4R3), numerous non-histone substrates have since been identified. The variety of these substrates underlines the essential role played by PRMT1 in a large number of biological processes such as transcriptional regulation, signal transduction or DNA repair. This review will provide an overview of the structural, biochemical and cellular features of PRMT1. After a description of the genomic organization and protein structure of PRMT1, special consideration was given to the regulation of PRMT1 enzymatic activity. Finally, we discuss the involvement of PRMT1 in embryonic development, DNA damage repair, as well as its participation in the initiation and progression of several types of cancers.
format Online
Article
Text
id pubmed-8619983
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-86199832021-11-27 Structure, Activity, and Function of PRMT1 Thiebaut, Charlène Eve, Louisane Poulard, Coralie Le Romancer, Muriel Life (Basel) Review PRMT1, the major protein arginine methyltransferase in mammals, catalyzes monomethylation and asymmetric dimethylation of arginine side chains in proteins. Initially described as a regulator of chromatin dynamics through the methylation of histone H4 at arginine 3 (H4R3), numerous non-histone substrates have since been identified. The variety of these substrates underlines the essential role played by PRMT1 in a large number of biological processes such as transcriptional regulation, signal transduction or DNA repair. This review will provide an overview of the structural, biochemical and cellular features of PRMT1. After a description of the genomic organization and protein structure of PRMT1, special consideration was given to the regulation of PRMT1 enzymatic activity. Finally, we discuss the involvement of PRMT1 in embryonic development, DNA damage repair, as well as its participation in the initiation and progression of several types of cancers. MDPI 2021-10-27 /pmc/articles/PMC8619983/ /pubmed/34833023 http://dx.doi.org/10.3390/life11111147 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Thiebaut, Charlène
Eve, Louisane
Poulard, Coralie
Le Romancer, Muriel
Structure, Activity, and Function of PRMT1
title Structure, Activity, and Function of PRMT1
title_full Structure, Activity, and Function of PRMT1
title_fullStr Structure, Activity, and Function of PRMT1
title_full_unstemmed Structure, Activity, and Function of PRMT1
title_short Structure, Activity, and Function of PRMT1
title_sort structure, activity, and function of prmt1
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619983/
https://www.ncbi.nlm.nih.gov/pubmed/34833023
http://dx.doi.org/10.3390/life11111147
work_keys_str_mv AT thiebautcharlene structureactivityandfunctionofprmt1
AT evelouisane structureactivityandfunctionofprmt1
AT poulardcoralie structureactivityandfunctionofprmt1
AT leromancermuriel structureactivityandfunctionofprmt1