Nucleic Acids Research Advance Access originally published online on August 21, 2008
Nucleic Acids Research 2008 36(17):5451-5461; doi:10.1093/nar/gkn519
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Nucleic Acids Research, 2008, Vol. 36, No. 17 5451-5461
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Genome integrity, repair and replication |
Viral AlkB proteins repair RNA damage by oxidative demethylation
1Department of Molecular Biosciences, University of Oslo, P.O. Box 1041 Blindern, N-0316 Oslo, Norway, 2National Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20894, 3Department of Botany and Plant Pathology, Center for Genome Research and Biocomputing, Oregon State University, Corvallis, OR 97331, USA and 4Centre for Molecular Biology and Neuroscience, Rikshospitalet-Radiumhospitalet HF, University of Oslo, Oslo, Norway
*To whom correspondence should be addressed. Tel: +47 22 85 48 40; Fax: +47 22 85 44 43; Email: pal.falnes{at}imbv.uio.no
Received June 23, 2008. Revised July 30, 2008. Accepted July 30, 2008.
Bacterial and mammalian AlkB proteins are iron(II)- and 2-oxoglutarate-dependent dioxygenases that reverse methylation damage, such as 1-methyladenine and 3-methylcytosine, in RNA and DNA. An AlkB-domain is encoded by the genome of numerous single-stranded, plant-infecting RNA viruses, the majority of which belong to the Flexiviridae family. Our phylogenetic analysis of AlkB sequences suggests that a single plant virus might have acquired AlkB relatively recently, followed by horizontal dissemination among other viruses via recombination. Here, we describe the first functional characterization of AlkB proteins from three plant viruses. The viral AlkB proteins efficiently reactivated methylated bacteriophage genomes when expressed in Escherichia coli, and also displayed robust, iron(II)- and 2-oxoglutarate-dependent demethylase activity in vitro. Viral AlkB proteins preferred RNA over DNA substrates, and thus represent the first AlkBs with such substrate specificity. Our results suggest a role for viral AlkBs in maintaining the integrity of the viral RNA genome through repair of deleterious methylation damage, and support the notion that AlkB-mediated RNA repair is biologically relevant.
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