RGG/RG Motif Regions in RNA Binding and Phase Separation |
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Authors: | P. Andrew Chong Robert M. Vernon Julie D. Forman-Kay |
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Affiliation: | 1. Program in Molecular Medicine, The Hospital for Sick Children, Toronto, ON, Canada;2. Department of Biochemistry, University of Toronto, Toronto, ON, Canada |
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Abstract: | RGG/RG motifs are RNA binding segments found in many proteins that can partition into membraneless organelles. They occur in the context of low-complexity disordered regions and often in multiple copies. Although short RGG/RG-containing regions can sometimes form high-affinity interactions with RNA structures, multiple RGG/RG repeats are generally required for high-affinity binding, suggestive of the dynamic, multivalent interactions that are thought to underlie phase separation in formation of cellular membraneless organelles. Arginine can interact with nucleotide bases via hydrogen bonding and π-stacking; thus, nucleotide conformers that provide access to the bases provide enhanced opportunities for RGG interactions. Methylation of RGG/RG regions, which is accomplished by protein arginine methyltransferase enzymes, occurs to different degrees in different cell types and may regulate the behavior of proteins containing these regions. |
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Keywords: | aDMA asymmetric dimethylarginine AdOx adenosine-2,3-dialdehyde EWS Ewing's sarcoma protein FET FUS, EWS, TAF15 FMRP fragile X mental retardation protein FUS fused in sarcoma GAR glycine–arginine rich G3BP1 Ras GTPase-activating protein-binding protein 1 hnRNP heterogenous nuclear ribonucleoprotein IDP intrinsically disordered protein IDR intrinsically disordered region LLPS liquid–liquid phase separation PAR poly(ADP-ribose) PDB Protein Data Bank PRMT protein arginine methyltransferase SERBP1 SERPINE1 mRNA-binding protein 1 TAF15 TATA binding associated factor 15 phase separation ribonucleoprotein granules GAR asymmetric dimethylation intrinsically disordered |
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