Endonuclease V cleaves at inosines in RNA

Erik Sebastian Vik, Meh Sameen Nawaz, Pernille Strøm Andersen, Cathrine Fladeby, Magnar Bjørås, Bjørn Dalhus and Ingrun Alseth ()
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Erik Sebastian Vik: Oslo University Hospital HF and University of Oslo
Meh Sameen Nawaz: Oslo University Hospital HF and University of Oslo
Pernille Strøm Andersen: Oslo University Hospital HF and University of Oslo
Cathrine Fladeby: Oslo University Hospital HF and University of Oslo
Magnar Bjørås: Oslo University Hospital HF and University of Oslo
Bjørn Dalhus: Oslo University Hospital HF and University of Oslo
Ingrun Alseth: Oslo University Hospital HF and University of Oslo

Nature Communications, 2013, vol. 4, issue 1, 1-7

Abstract: Abstract Endonuclease V orthologues are highly conserved proteins found in all kingdoms of life. While the prokaryotic enzymes are DNA repair proteins for removal of deaminated adenosine (inosine) from the genome, no clear role for the eukaryotic counterparts has hitherto been described. Here we report that human endonuclease V (ENDOV) and also Escherichia coli endonuclease V are highly active ribonucleases specific for inosine in RNA. Inosines are normal residues in certain RNAs introduced by specific deaminases. Adenosine-to-inosine editing is essential for proper function of these transcripts and defects are linked to various human disease. Here we show that human ENDOV cleaves an RNA substrate containing inosine in a position corresponding to a biologically important site for deamination in the Gabra-3 transcript of the GABAA neurotransmitter. Further, human ENDOV specifically incises transfer RNAs with inosine in the wobble position. This previously unknown RNA incision activity may suggest a role for endonuclease V in normal RNA metabolism.

Date: 2013
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DOI: 10.1038/ncomms3271

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