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 journalArticle

33 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)7984-7996
Number of pages13
JournalNucleic Acids Research
Volume45
Issue number13
DOIs
StatePublished - Jul 1 2017

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Sarcoma
RNA
Human Genome

ASJC Scopus subject areas

  • Genetics

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Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding. / Ozdilek, Bagdeser A.; Thompson, Valery F.; Ahmed, Nasiha S.; White, Connor I.; Batey, Robert T.; Schwartz, Jacob C.

In: Nucleic Acids Research, Vol. 45, No. 13, 01.07.2017, p. 7984-7996.

Research output: Contribution to journalArticle

Ozdilek, Bagdeser A. ; Thompson, Valery F. ; Ahmed, Nasiha S. ; White, Connor I. ; Batey, Robert T. ; Schwartz, Jacob C. / Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding. In: Nucleic Acids Research. 2017 ; Vol. 45, No. 13. pp. 7984-7996.
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