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Nucleic Acids Res. 2017 Jul 27;45(13):7984-7996. doi: 10.1093/nar/gkx460.

Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding.

Author information

1
Department of Molecular, Cellular and Developmental Biology, University of Colorado, Campus Box 347, Boulder, CO 80309, USA.
2
Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, USA.
3
Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721, USA.
4
Department of Chemistry and Biochemistry, University of Colorado, Campus Box 596, Boulder, CO 80309, USA.

Abstract

RGG/RG domains are the second most common RNA binding domain in the human genome, yet their RNA-binding properties remain poorly understood. Here, we report a detailed analysis of the RNA binding characteristics of intrinsically disordered RGG/RG domains from Fused in Sarcoma (FUS), FMRP and hnRNPU. For FUS, previous studies defined RNA binding as mediated by its well-folded domains; however, we show that RGG/RG domains are the primary mediators of binding. RGG/RG domains coupled to adjacent folded domains can achieve affinities approaching that of full-length FUS. Analysis of RGG/RG domains from FUS, FMRP and hnRNPU against a spectrum of contrasting RNAs reveals that each display degenerate binding specificity, while still displaying different degrees of preference for RNA.

PMID:
28575444
PMCID:
PMC5570134
DOI:
10.1093/nar/gkx460
[Indexed for MEDLINE]
Free PMC Article

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