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NUDT2 initiates viral RNA degradation by removal of 5'-phosphates.
Laudenbach, Beatrice T Krey, Karsten Emslander, Quirin Andersen, Line Lykke Reim, Alexander Scaturro, Pietro Mundigl, Sarah Dächert, Christopher Manske, Katrin Moser, Markus
Laudenbach, Beatrice T
Krey, Karsten
Emslander, Quirin
Andersen, Line Lykke
Reim, Alexander
Scaturro, Pietro
Mundigl, Sarah
Dächert, Christopher
Manske, Katrin
Moser, Markus
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2021-11-25
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Abstract
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.
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Nat Commun. 2021 Nov 25;12(1):6918. doi: 10.1038/s41467-021-27239-y.
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en
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2041-1723
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Attribution 4.0 International