Protein arginine methylation of viral proteins

Protein arginine methylation of viral proteins

Protein arginine methyltransferases (PRMTs) can catalyze the addition of methyl groups to the nitrogen atoms of specific arginine residues in proteins. The major cellular substrates modified by PRMTs are nucleic acid-binding proteins mostly with the glycine and arginine-rich (GAR) motifs. Through modulating the interaction of protein or RNA, protein arginine methylation is important for the regulation of liquid-liquid phase separation to form ribonucleoparticles (RNPs) and membrane-less organelles (MLOs) such as nucleoli and stress granules. The same principle can be applied to viral proteins when they are arginine methylated to modulate processes in the viral life cycle and particle assembly. This review summarizes the arginine methylation of viral proteins across different types of viruses. We also used a GAR Motif Finder program to analyze the arginine-methylated viral proteins and some viral proteomes. A portion of viral proteins contain GAR motifs but some viral arginine methylated proteins do not have GAR motifs. The arginine methylation of viral proteins affects different aspects of viral life cycles, such as viral replication, gene expression, protein stability, RNA binding, and subcellular localization. Targeting arginine methylation thus has the potential as a therapeutic strategy for antiviral interventions.