Nucleic Acids Research
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.
Ozdilek, Bagdeser A; Thompson, Valery F; Ahmed, Nasiha S; White, Connor I; Batey, Robert T; and Schwartz, Jacob C, "Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding." (2017). Chemistry & Biochemistry Faculty Contributions. 98.