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Despite the odds: Formation of the SARS-CoV-2 methylation complex.
Nucleic Acids Res. 52, 6441-6458 (2024)
Coronaviruses modify their single-stranded RNA genome with a methylated cap during replication to mimic the eukaryotic mRNAs. The capping process is initiated by several nonstructural proteins (nsp) encoded in the viral genome. The methylation is performed by two methyltransferases, nsp14 and nsp16, while nsp10 acts as a co-factor to both. Additionally, nsp14 carries an exonuclease domain which operates in the proofreading system during RNA replication of the viral genome. Both nsp14 and nsp16 were reported to independently bind nsp10, but the available structural information suggests that the concomitant interaction between these three proteins would be impossible due to steric clashes. Here, we show that nsp14, nsp10, and nsp16 can form a heterotrimer complex upon significant allosteric change. This interaction is expected to encourage the formation of mature capped viral mRNA, modulating nsp14's exonuclease activity, and protecting the viral RNA. Our findings show that nsp14 is amenable to allosteric regulation and may serve as a novel target for therapeutic approaches.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Structural Basis; Protein; Exoribonuclease; Replication; Reveals; Nsp14; Domain
ISSN (print) / ISBN
0305-1048
e-ISSN
1362-4962
Zeitschrift
Nucleic Acids Research
Quellenangaben
Band: 52,
Heft: 11,
Seiten: 6441-6458
Verlag
Oxford University Press
Verlagsort
Great Clarendon St, Oxford Ox2 6dp, England
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)
Förderungen
Jagiellonian University in Krakow