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Nucleic Acids Research 2005 33(16):5362-5370; doi:10.1093/nar/gki849
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Published online 21 September 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

Modulation of ADAR1 editing activity by Z-RNA in vitro

Michael Koeris1,2, Lars Funke1, Jay Shrestha1, Alexander Rich1 and Stefan Maas3,*

1Department of Biology, Massachusetts Institute of Technology Cambridge, MA 02142, USA 2Institut für Biochemie, Freie Universität Berlin Germany 3Department of Biological Sciences, Lehigh University Bethlehem, PA 18015, USA

*To whom correspondence should be addressed. Tel: +1 610 758 6276; Fax: +1 610 758 4004; Email: swm3{at}lehigh.edu

Received July 21, 2005. Revised September 1, 2005. Accepted September 1, 2005.

RNA editing by A-to-I modification has been recognized as an important molecular mechanism for generating RNA and protein diversity. In mammals, it is mediated by a family of adenosine deaminases that act on RNAs (ADARs). The large version of the editing enzyme ADAR1 (ADAR1-L), expressed from an interferon-responsible promoter, has a Z-DNA/Z-RNA binding domain at its N-terminus. We have tested the in vitro ability of the enzyme to act on a 50 bp segment of dsRNA with or without a Z-RNA forming nucleotide sequence. A-to-I editing efficiency is markedly enhanced in presence of the sequence favoring Z-RNA. In addition, an alteration in the pattern of modification along the RNA duplex becomes evident as reaction times decrease. These results suggest that the local conformation of dsRNA molecules might be an important feature for target selectivity by ADAR1 and other proteins with Z-RNA binding domains.

Present addresses: Lars Funke, Department of Physiology, University of California, San Francisco, CA, USA

Jay Shrestha, Department of Molecular Genetics and Cell Biology at the University of Chicago, Chicago, IL, USA


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