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dc.contributor.authorOzdilek, Bagdeser A.*
dc.contributor.authorThompson, Valery F.*
dc.contributor.authorAhmed, Nasiha S.*
dc.contributor.authorWhite, Connor I.*
dc.contributor.authorBatey, Robert T.*
dc.contributor.authorSchwartz, Jacob C.*
dc.date.accessioned2017-09-07T16:24:02Z
dc.date.available2017-09-07T16:24:02Z
dc.date.issued2017-07-27
dc.identifier.citationIntrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding 2017, 45 (13):7984 Nucleic Acids Researchen
dc.identifier.issn0305-1048
dc.identifier.issn1362-4962
dc.identifier.doi10.1093/nar/gkx460
dc.identifier.urihttp://hdl.handle.net/10150/625471
dc.description.abstractRGG/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.
dc.description.sponsorshipMinistry 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]en
dc.language.isoenen
dc.publisherOXFORD UNIV PRESSen
dc.relation.urlhttps://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkx460en
dc.rights© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License.en
dc.titleIntrinsically disordered RGG/RG domains mediate degenerate specificity in RNA bindingen
dc.typeArticleen
dc.contributor.departmentUniv Arizona, Dept Chem & Biochemen
dc.contributor.departmentUniv Arizona, Dept Mol & Cellular Biolen
dc.identifier.journalNucleic Acids Researchen
dc.description.noteOpen access journal.en
dc.description.collectioninformationThis item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.en
dc.eprint.versionFinal published versionen
refterms.dateFOA2018-07-13T04:08:51Z
html.description.abstractRGG/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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