Journal
NUCLEIC ACIDS RESEARCH
Volume 45, Issue 13, Pages 7984-7996Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkx460
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Funding
- Ministry of Education of Turkey Fellowship
- National Institute of General Medical Sciences [T32-GM008659]
- National Institutes of Health [R01 GM12008118, R00 NS082376]
- National Institute of Neurological Disorders and Stroke [R00 NS082376]
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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.
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