Format

Send to

Choose Destination
Nat Commun. 2013;4:2271. doi: 10.1038/ncomms3271.

Endonuclease V cleaves at inosines in RNA.

Author information

1
Department of Microbiology, Oslo University Hospital HF and University of Oslo, Rikshospitalet, PO Box 4950 Nydalen, 0424 Oslo, Norway.

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 GABA(A) 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.

PMID:
23912683
PMCID:
PMC3741635
DOI:
10.1038/ncomms3271
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central Icon for Norwegian BIBSYS system
Loading ...
Support Center