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NMPylation and de-NMPylation of SARS-CoV-2 nsp9 by the NiRAN domain

Nucleic Acids Res. 2021-09; 
Bing Wang, Dmitri Svetlov, Irina Artsimovitch
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Custom Vector Construction … coli and synthesized by GenScript and subcloned into standard pET-derived expression vectors under control of the T7 gene 10 promoter and lac repressor. The derivative plasmids were constructed by standard molecular biology approaches with restriction and modification … Get A Quote

摘要

The catalytic subunit of SARS-CoV-2 RNA-dependent RNA polymerase (RdRp) contains two active sites that catalyze nucleotidyl-monophosphate transfer (NMPylation). Mechanistic studies and drug discovery have focused on RNA synthesis by the highly conserved RdRp. The second active site, which resides in a Nidovirus RdRp-Associated Nucleotidyl transferase (NiRAN) domain, is poorly characterized, but both catalytic reactions are essential for viral replication. One study showed that NiRAN transfers NMP to the first residue of RNA-binding protein nsp9; another reported a structure of nsp9 containing two additional N-terminal residues bound to the NiRAN active site but observed NMP transfer to RNA instead. We show that... More

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