Human endonuclease V is a ribonuclease specific for inosine-containing RNA

Yoko Morita, Toshihiro Shibutani, Nozomi Nakanishi, Kazuko Nishikura, Shigenori Iwai and Isao Kuraoka ()
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Yoko Morita: Graduate School of Engineering Science, Osaka University
Toshihiro Shibutani: Graduate School of Engineering Science, Osaka University
Nozomi Nakanishi: Graduate School of Engineering Science, Osaka University
Kazuko Nishikura: The Wistar Institute
Shigenori Iwai: Graduate School of Engineering Science, Osaka University
Isao Kuraoka: Graduate School of Engineering Science, Osaka University

Nature Communications, 2013, vol. 4, issue 1, 1-10

Abstract: Abstract Deamination of DNA bases can create missense mutations predisposing humans to cancer and also interfere with other basic molecular genetic processes; this deamination generates deoxyinosine from deoxyadenosine. In Escherichia coli, the highly conserved endonuclease V is involved in alternative excision repair that removes deoxyinosine from DNA. However, its exact activities and roles in humans are unknown. Here we characterize the FLJ35220 protein, the human homologue of E. coli endonuclease V, hEndoV as a ribonuclease specific for inosine-containing RNA. hEndoV preferentially binds to RNA and efficiently hydrolyses the second phosphodiester bond located 3′ to the inosine in unpaired inosine-containing ssRNA regions in dsRNA. It localizes to the cytoplasm in cells. The ribonuclease activity is promoted by Tudor staphylococcal nuclease and detected on inosine-containing dsRNA created by the action of adenosine deaminases acting on RNA. These results demonstrate that hEndoV controls the fate of inosine-containing RNA in humans.

Date: 2013
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DOI: 10.1038/ncomms3273

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