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J Mol Biol. 2018 Nov 2;430(23):4650-4665. doi: 10.1016/j.jmb.2018.06.014. Epub 2018 Jun 15.

RGG/RG Motif Regions in RNA Binding and Phase Separation.

Author information

1
Program in Molecular Medicine, The Hospital for Sick Children, Toronto, ON, Canada.
2
Program in Molecular Medicine, The Hospital for Sick Children, Toronto, ON, Canada; Department of Biochemistry, University of Toronto, Toronto, ON, Canada. Electronic address: forman@sickkids.ca.

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.

KEYWORDS:

GAR; asymmetric dimethylation; intrinsically disordered; phase separation; ribonucleoprotein granules

PMID:
29913160
DOI:
10.1016/j.jmb.2018.06.014
[Indexed for MEDLINE]

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