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Nucleic Acids Research 2005 33(18):5954-5964; doi:10.1093/nar/gki909
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Published online 27 October 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

Cleavage of dsRNAs hyper-edited by ADARs occurs at preferred editing sites

A. D. J. Scadden* and M. A. O'Connell1

University of Cambridge 80 Tennis Court Road, Cambridge, CB2 1GA, UK 1MRC Human Genetics Unit, Western General Hospital Crewe Road, Edinburgh, EH4 2XU, UK

*To whom correspondence should be addressed. Tel: +44 1223 333665; Fax: +44 1223 766002; Email: adjs{at}bioc.cam.ac.uk

Received September 9, 2005. Revised September 30, 2005. Accepted September 30, 2005.

Long double-stranded RNAs (dsRNAs) may undergo covalent modification (hyper-editing) by adenosine deaminases that act on RNA (ADARs), whereby up to 50–60% of adenosine residues are converted to inosine. Previously, we have described a ribonuclease activity in various cell extracts that specifically targets dsRNAs hyper-edited by ADARs. Such a ribonuclease may play an important role in viral defense, or may alternatively be involved in down-regulation of other RNA duplexes. Cleavage of hyper-edited dsRNA occurs within sequences containing multiple IU pairs but not in duplexes that contain either isosteric GU pairs or Watson–Crick base pairs. Here, we describe experiments aimed at further characterizing cleavage of hyper-edited dsRNA. Using various inosine-containing dsRNAs we show that cleavage occurs preferentially at a site containing both IU and UI pairs, and that inclusion of even a single GU pair inhibits cleavage. We also show that cleavage occurs on both strands within a single dsRNA molecule and requires a 2'-OH group. Strikingly, we show that ADAR1, ADAR2 or dADAR all preferentially generate the preferred cleavage site when hyper-editing a long dsRNA.


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