Description
Title: JMJD5-JMJD6-JMJD7’s Novel Protease Activities and Arginine Methyltransferases’ Arginine Methylation Activities Are Probably coupled.
Abstract: The unexpected identification of the protease activities on arginine-methylated targets by JMJD5, JMJD6, and JMJD7, members of a subfamily of Jumonji domain-containing family, raises several concerns about their veracity, significance, and relationships with other proteins. Although the arginine methyltransferase family (PRMTs) appears to play crucial roles in the regulation of transcription, including the activation and inactivation of a large group of genes, as well as other biological activities, the precise function of this protein family is still unknown despite decades of research and a massive accumulation of data. In this review, we hope to clarify how JMJD5/6/7 and PRMTs likely have a coupled function. In addition to their roles in controlling the biogenesis of membrane-free organelles in cells, stimulating transcription factors play a significant role in controlling the activities of RNA Polymerase II in higher eukaryotes, particularly in the animal kingdom. Furthermore, we suggest that a subfamily of the Jumonji protein family may target the ubiquitous PRMT methylation of arginine as a target for destruction after missions.
Keywords: JMJD5; JMJD6; JMJD7; Jumonji; PRMT
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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