Protein arginine methyltransferase 1 regulates herpes simplex virus replication through ICP27 RGG-box methylation

Biochemical and Biophysical Research Communications
Jungeun YuJaerang Rho

Abstract

Protein arginine methylation is involved in viral infection and replication through the modulation of diverse cellular processes including RNA metabolism, cytokine signaling, and subcellular localization. It has been suggested previously that the protein arginine methylation of the RGG-box of ICP27 is required for herpes simplex virus type-1 (HSV-1) viral replication and gene expression in vivo. However, a cellular mediator for this process has not yet been identified. In our current study, we show that the protein arginine methyltransferase 1 (PRMT1) is a cellular mediator of the arginine methylation of ICP27 RGG-box. We generated arginine substitution mutants in this domain and examined which arginine residues are required for methylation by PRMT1. R138, R148 and R150 were found to be the major sites of this methylation but additional arginine residues serving as minor methylation sites are still required to sustain the fully methylated form of ICP27 RGG. We also demonstrate that the nuclear foci-like structure formation, SRPK interactions, and RNA-binding activity of ICP27 are modulated by the arginine methylation of the ICP27 RGG-box. Furthermore, HSV-1 replication is inhibited by hypomethylation of this domain resulting fr...Continue Reading

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Citations

May 26, 2012·Journal of Genetics and Genomics = Yi Chuan Xue Bao·Ayaz Ahmad, Xiaofeng Cao
Oct 24, 2019·MBio·Richard B TunnicliffeAlexander P Golovanov
Aug 2, 2019·Journal of Applied Physiology·Tiffany L vanLieshoutVladimir Ljubicic
May 8, 2020·Current Protein & Peptide Science·Ayad A Al-HamashiRong Huang
Mar 31, 2015·Journal of Proteome Research·Alicia R BerardAlberto Severini

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