Article
Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding. Public 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
- Last Modified
- 2019-12-05
- Identifier
- PubMed ID: 28575444
- Resource Type
- Rights Statement
- DOI
- ISSN
- 1362-4962
- Language
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