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

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https://scholar.colorado.edu/concern/articles/br86b423c
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.
Creator
Date Issued
  • 2017-07-27
Academic Affiliation
Journal Title
Journal Issue/Number
  • 13
Journal Volume
  • 45
File Extent
  • 7984-7996
Subject
Publisher
Última modificação
  • 2019-12-05
Identifier
  • PubMed ID: 28575444
Resource Type
Declaração de direitos
DOI
ISSN
  • 1362-4962
Language

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