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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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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 |
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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 |
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