Endonuclease V cleaves at inosines in RNA
| Autor: | Ingrun Alseth, Pernille Strøm Andersen, Magnar Bjørås, Bjørn Dalhus, Cathrine Fladeby, Meh Sameen Nawaz, Erik Sebastian Vik |
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| Rok vydání: | 2013 |
| Předmět: |
DNA repair
General Physics and Astronomy General Biochemistry Genetics and Molecular Biology Article Substrate Specificity Deoxyribonuclease (Pyrimidine Dimer) RNA Transfer Endonuclease V Cell Line Tumor Escherichia coli Humans Ribonuclease chemistry.chemical_classification RNA metabolism Multidisciplinary biology RNA General Chemistry DNA Molecular biology Inosine Enzyme chemistry Biochemistry biology.protein |
| Zdroj: | Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | 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. Bacterial endonuclease V enzymes are characterized as DNA repair proteins. Here the authors show that human endonuclease V is an inosine-specific ribonuclease, indicating a role for this enzyme in normal RNA metabolism rather than DNA repair. |
| Databáze: | OpenAIRE |
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