Key result
Cryo-EM analysis revealed an alternative, dimeric form of the SARS-CoV-2 RNA-dependent RNA polymerase at 5.5 Å resolution, which may facilitate template switching during sub-genomic RNA production.
The coronavirus SARS-CoV-2 uses an RNA-dependent RNA polymerase (RdRp) to replicate and transcribe its genome. Previous structures of the RdRp revealed a monomeric enzyme composed of the catalytic subunit nsp12, two copies of subunit nsp8, and one copy of subunit nsp7. Here we report an alternative, dimeric form of the enzyme and resolve its structure at 5.5 Å resolution. In this structure, the two RdRps contain only one copy of nsp8 each and dimerize via their nsp7 subunits to adopt an antiparallel arrangement. We speculate that the RdRp dimer facilitates template switching during production of sub-genomic RNAs.
No takes yet. Share an insight, caveat, or question.
Jochheim et al. (2021) studied SARS-CoV-2. Cryo-EM structural analysis was evaluated on Structure of SARS-CoV-2 RdRp dimer. Cryo-EM analysis revealed an alternative, dimeric form of the SARS-CoV-2 RNA-dependent RNA polymerase at 5.5 Å resolution, which may facilitate template switching during sub-genomic RNA production.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: