Protein arginine methyltransferase 1, a major regulator of biological processes.

Biochem Cell Biol

Department of Biochemistry and Medical Genetics, Max Rady College of Medicine, Rady Faculty of Health Sciences, University of Manitoba, MB, Canada.

Published: April 2024

AI Article Synopsis

  • PRMT1 is a key enzyme that adds methyl groups to arginine residues in proteins, initially recognized for its role in modifying histone H4 to regulate gene expression.
  • This enzyme influences various biological processes, including chromatin dynamics, transcription, RNA processing, and signal transduction by acting on multiple protein substrates.
  • The review covers PRMT1's structure, regulation, interactions with other proteins, and its implications in health and disease, especially its role in splicing and involvement with related genes.

Article Abstract

Protein arginine methyltransferase 1 (PRMT1) is a major type I arginine methyltransferase that catalyzes the formation of monomethyl and asymmetric dimethylarginine in protein substrates. It was first identified to asymmetrically methylate histone H4 at the third arginine residue forming the H4R3me2a active histone mark. However, several protein substrates are now identified as being methylated by PRMT1. As a result of its association with diverse classes of substrates, PRMT1 regulates several biological processes like chromatin dynamics, transcription, RNA processing, and signal transduction. The review provides an overview of PRMT1 structure, biochemical features, specificity, regulation, and role in cellular functions. We discuss the genomic distribution of PRMT1 and its association with genes. Further, we explore the different substrates of PRMT1 involved in splicing. In the end, we discuss the proteins that interact with PRMT1 and their downstream effects in diseased states.

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Source
http://dx.doi.org/10.1139/bcb-2023-0212DOI Listing

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