NUDT2 initiates viral RNA degradation by removal of 5'-phosphates.
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Authors
Laudenbach, Beatrice TKrey, Karsten
Emslander, Quirin
Andersen, Line Lykke
Reim, Alexander
Scaturro, Pietro
Mundigl, Sarah
Dächert, Christopher
Manske, Katrin
Moser, Markus
Ludwig, Janos
Wohlleber, Dirk
Kröger, Andrea
Binder, Marco
Pichlmair, Andreas
Issue Date
2021-11-25
Metadata
Show full item recordAbstract
While viral replication processes are largely understood, comparably little is known on cellular mechanisms degrading viral RNA. Some viral RNAs bear a 5'-triphosphate (PPP-) group that impairs degradation by the canonical 5'-3' degradation pathway. Here we show that the Nudix hydrolase 2 (NUDT2) trims viral PPP-RNA into monophosphorylated (P)-RNA, which serves as a substrate for the 5'-3' exonuclease XRN1. NUDT2 removes 5'-phosphates from PPP-RNA in an RNA sequence- and overhang-independent manner and its ablation in cells increases growth of PPP-RNA viruses, suggesting an involvement in antiviral immunity. NUDT2 is highly homologous to bacterial RNA pyrophosphatase H (RppH), a protein involved in the metabolism of bacterial mRNA, which is 5'-tri- or diphosphorylated. Our results show a conserved function between bacterial RppH and mammalian NUDT2, indicating that the function may have adapted from a protein responsible for RNA turnover in bacteria into a protein involved in the immune defense in mammals.Citation
Nat Commun. 2021 Nov 25;12(1):6918. doi: 10.1038/s41467-021-27239-y.Affiliation
HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.Publisher
Springer NatureJournal
Nature communicationsPubMed ID
34824277Type
ArticleLanguage
enEISSN
2041-1723ae974a485f413a2113503eed53cd6c53
10.1038/s41467-021-27239-y
Scopus Count
The following license files are associated with this item:
- Creative Commons
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