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. 2023 Jul 28;51(16):8677–8690. doi: 10.1093/nar/gkad627

Figure 1.

Figure 1.

(A) Cartoon representing the peptide sequence of SARS-CoV-2 NSP1. The protein consists of three domains, a long NTD (1–116), a hinge domain (117–149) and a CTD (150–180). In this study, we purified recombinant NSP1 wt and four mutants. The amino acid substitutions and the positions of the mutations are indicated above the cartoon. In the CTD, two helices called α1 and α2 are shown in grey; they are required for ribosome binding. (B) The cartoon represents three types of RNA substrates. First, chimeric RNAs containing the 5′UTR of cellular mRNAs (ISG54, IL-8, VIPERIN, ISG15, RIG-I and β-globin) inserted upstream of the N-terminal part of the Renilla luciferase coding sequence, second chimeric RNA containing the 5′UTR of SARS-CoV-2 subgenomic RNA coding for the nucleocapsid (CoV2-sub-N) and third chimeric RNA containing the 5′UTR of the SARS-CoV-2 genomic RNA (Cov2-gen). (C) RNA degradation assay of various reporter mRNAs. The full-length 5′-labelled RNA transcripts are incubated for 5 min at 30°C in the presence of RRL in the absence (Ø) or presence of 0.1 and 0.5 μM wt NSP1 protein and analysed by denaturing 12% PAGE.