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

Bagdeser A. Ozdilek, Valery F. Thompson, Nasiha S. Ahmed, Connor I. White, Robert T. Batey, Jacob C. Schwartz

Research output: Contribution to journalArticlepeer-review

133 Scopus citations


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 languageEnglish (US)
Pages (from-to)7984-7996
Number of pages13
JournalNucleic acids research
Issue number13
StatePublished - Jul 1 2017

ASJC Scopus subject areas

  • Genetics


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