dc.contributor.authorWashburn, Michael C.
dc.contributor.authorKakaradov, Boyko.
dc.contributor.authorSundararaman, Balaji.
dc.contributor.authorWheeler, Emily.
dc.contributor.authorHoon, Shawn.
dc.contributor.authorYeo, Gene W.
dc.contributor.authorHundley, Heather A.
dc.date.accessioned2014-02-19T03:58:29Z
dc.date.available2014-02-19T03:58:29Z
dc.date.copyright2014en_US
dc.date.issued2014
dc.identifier.citationWashburn, M. C., Kakaradov, B., Sundararaman, B., Wheeler, E., Hoon, S., Yeo, G. W., et al. (2014). The dsRBP and inactive editor ADR-1 utilizes dsRNA binding to regulate A-to-I RNA editing across the C. elegans transcriptome. Cell reports, 6, 1-9.en_US
dc.identifier.issn2211-1247en_US
dc.identifier.urihttp://hdl.handle.net/10220/18837
dc.description.abstractInadequate adenosine-to-inosine editing of noncoding regions occurs in disease but is often uncorrelated with ADAR levels, underscoring the need to study deaminase-independent control of editing. C. elegans have two ADAR proteins, ADR-2 and the theoretically catalytically inactive ADR-1. Using high-throughput RNA sequencing of wild-type and adr mutant worms, we expand the repertoire of C. elegans edited transcripts over 5-fold and confirm that ADR-2 is the only active deaminase in vivo. Despite lacking deaminase function, ADR-1 affects editing of over 60 adenosines within the 3′ UTRs of 16 different mRNAs. Furthermore, ADR-1 interacts directly with ADR-2 substrates, even in the absence of ADR-2, and mutations within its double-stranded RNA (dsRNA) binding domains abolish both binding and editing regulation. We conclude that ADR-1 acts as a major regulator of editing by binding ADR-2 substrates in vivo. These results raise the possibility that other dsRNA binding proteins, including the inactive human ADARs, regulate RNA editing through deaminase-independent mechanisms.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesCell reportsen_US
dc.rights© 2014 The Authors. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License, which permits non-commercial use, distribution, and reproduction in any medium, provided the original author and source are credited.en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleThe dsRBP and inactive editor ADR-1 utilizes dsRNA binding to regulate A-to-I RNA editing across the C. elegans transcriptomeen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1016/j.celrep.2014.01.011
dc.description.versionPublished versionen_US


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