Structure, Activity, and Function of PRMT1

Autor: Charlène Thiebaut, Louisane Eve, Coralie Poulard, Muriel Le Romancer
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Zdroj: Life, Vol 11, Iss 11, p 1147 (2021)
Druh dokumentu: article
ISSN: 2075-1729
DOI: 10.3390/life11111147
Popis: 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.
Databáze: Directory of Open Access Journals
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