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TitleCharacterization of SARS2 Nsp15 nuclease activity reveals it's mad about U.
Journal, issue, pagesNucleic Acids Res, Vol. 49, Issue 17, Page 10136-10149, Year 2021
Publish dateSep 27, 2021
AuthorsMeredith N Frazier / Lucas B Dillard / Juno M Krahn / Lalith Perera / Jason G Williams / Isha M Wilson / Zachary D Stewart / Monica C Pillon / Leesa J Deterding / Mario J Borgnia / Robin E Stanley /
PubMed AbstractNsp15 is a uridine specific endoribonuclease that coronaviruses employ to cleave viral RNA and evade host immune defense systems. Previous structures of Nsp15 from across Coronaviridae revealed that ...Nsp15 is a uridine specific endoribonuclease that coronaviruses employ to cleave viral RNA and evade host immune defense systems. Previous structures of Nsp15 from across Coronaviridae revealed that Nsp15 assembles into a homo-hexamer and has a conserved active site similar to RNase A. Beyond a preference for cleaving RNA 3' of uridines, it is unknown if Nsp15 has any additional substrate preferences. Here, we used cryo-EM to capture structures of Nsp15 bound to RNA in pre- and post-cleavage states. The structures along with molecular dynamics and biochemical assays revealed critical residues involved in substrate specificity, nuclease activity, and oligomerization. Moreover, we determined how the sequence of the RNA substrate dictates cleavage and found that outside of polyU tracts, Nsp15 has a strong preference for purines 3' of the cleaved uridine. This work advances our understanding of how Nsp15 recognizes and processes viral RNA, and will aid in the development of new anti-viral therapeutics.
External linksNucleic Acids Res / PubMed:34403466 / PubMed Central
MethodsEM (single particle)
Resolution2.2 - 2.5 Å
Structure data

24101

7n06

EMDB-24101, PDB-7n06:
SARS-CoV-2 Nsp15 endoribonuclease post-cleavage state
Method: EM (single particle) / Resolution: 2.2 Å

24137

7n33

EMDB-24137, PDB-7n33:
SARS-CoV-2 Nsp15 endoribonuclease pre-cleavage state
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / Hydrolase/RNA / endoribonuclease / Hydrolase-RNA complex / VIRAL PROTEIN/RNA / VIRAL PROTEIN-RNA complex

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