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...

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Autores principales:	Thiebaut Charlène, Eve Louisane, Poulard Coralie, Le Romancer Muriel
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	PRMT1 arginine methylation H4R3 methylation transcriptional regulation cell signaling DNA damage repair Science Q
Acceso en línea:	https://doaj.org/article/89fd1e5237a942578239676696c2e1c5
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spelling	oai:doaj.org-article:89fd1e5237a942578239676696c2e1c52021-11-25T18:10:39ZStructure, Activity, and Function of PRMT110.3390/life111111472075-1729https://doaj.org/article/89fd1e5237a942578239676696c2e1c52021-10-01T00:00:00Zhttps://www.mdpi.com/2075-1729/11/11/1147https://doaj.org/toc/2075-1729PRMT1, 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.Thiebaut CharlèneEve LouisanePoulard CoralieLe Romancer MurielMDPI AGarticlePRMT1arginine methylationH4R3 methylationtranscriptional regulationcell signalingDNA damage repairScienceQENLife, Vol 11, Iss 1147, p 1147 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	PRMT1 arginine methylation H4R3 methylation transcriptional regulation cell signaling DNA damage repair Science Q
spellingShingle	PRMT1 arginine methylation H4R3 methylation transcriptional regulation cell signaling DNA damage repair Science Q Thiebaut Charlène Eve Louisane Poulard Coralie Le Romancer Muriel Structure, Activity, and Function of PRMT1
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	article
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
title	Structure, Activity, and Function of PRMT1
title_short	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_sort	structure, activity, and function of prmt1
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/89fd1e5237a942578239676696c2e1c5
work_keys_str_mv	AT thiebautcharlene structureactivityandfunctionofprmt1 AT evelouisane structureactivityandfunctionofprmt1 AT poulardcoralie structureactivityandfunctionofprmt1 AT leromancermuriel structureactivityandfunctionofprmt1
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Structure, Activity, and Function of PRMT1

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