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 wellfolded 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.
Original language | English (US) |
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Pages (from-to) | 7984-7996 |
Number of pages | 13 |
Journal | Nucleic acids research |
Volume | 45 |
Issue number | 13 |
DOIs | |
State | Published - Jul 1 2017 |
ASJC Scopus subject areas
- Genetics