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Despite the odds: formation of the SARS-CoV-2 methylation complex

Author information

Affiliations

  • 1. Virogenetics Laboratory of Virology, Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7a, 30-387 Krakow, Poland
      Authors
    • Matsuda A 1
    • Plewka J 1
    • Chykunova Y 1
    • Pachota M 1
    • Rawski M 1
    • Karim A 1
    • Kresik L 1
    • Lis K 1
    • Pyrć K 1
    • Czarna A 1
    (10 authors)
  • 2. Helmholtz Zentrum München, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany
      Authors
    • Jones AN 2
    • Mourão A 2
    • Sattler M 2
    • Popowicz GM 2
    (4 authors)
  • 3. Max Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin Institute for Medical Systems Biology, Berlin 13125, Germany
      Authors
    • Minia I 3
    (1 author)
  • 4. Department of Analytical Chemistry and Biochemistry, Faculty of Materials Science and Ceramics, AGH University of Science and Technology, Mickiewicza 30, 30-059 Krakow, Poland
      Authors
    • Hartman K 4
    • Suder P 4
    (2 authors)
  • 5. Protein Crystallography Research Group, Malopolska Centre of Biotechnology, Jagiellonian University, Gronostajowa 7a, 30-387 Krakow, Poland
      Authors
    • Sonani R 5
    • Dubin G 5
    (2 authors)
    • Show all (6)

ORCIDs linked to this article

Show all (6)

Preprint from bioRxiv, 26 Jan 2022
https://doi.org/10.1101/2022.01.25.477673 PPR: PPR446917 

Preprint

This article is a preprint. A journal published article is available.

Abstract 

Coronaviruses protect their single-stranded RNA genome with a methylated cap during replication. 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 where nsp10 acts as a co-factor to both. Aditionally, 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 should be impossible due to steric clashes. Here, we show that nsp14, nsp10, and nsp16 can form a heterotrimer complex. This interaction is expected to encourage formation of mature capped viral mRNA, modulating the 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.

Full text links 

Read article at publisher's site: https://doi.org/10.1101/2022.01.25.477673

Read article for free, from open access legal sources, via Unpaywall: https://academic.oup.com/nar/advance-article-pdf/doi/10.1093/nar/gkae165/57009122/gkae165.pdfUnpaywall

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Data 

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Genes & Proteins (2)

Protein structures in PDBe (4)