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. 2022 Aug 9;609(7928):793–800. doi: 10.1038/s41586-022-05185-z

Fig. 3. The NiRAN domain catalyses the transfer of 5′-pRNA from nsp9 to GDP to form the core cap structure GpppA-RNA.

Fig. 3

a, DeRNAylation of the covalent nsp9–RNALS10 species by WT nsp12, the NiRAN mutant (D218A) or the polymerase mutant (D760A) when incubated with buffer or GDP. The reaction products were analysed as described in Fig. 2b. b, Time-dependent deRNAylation of nsp9–pRNALS10 by WT nsp12, the NiRAN mutant (D218A) or the polymerase mutant (D760A). The reaction products were analysed as described in Fig. 2b. c, DeRNAylation of nsp9–pRNALS10 by nsp12 in the presence of different NTPs, NDPs or PPi. The reaction products were analysed as described in Fig. 2b. d, Incorporation of α-32P from [α-32P]GDP into nsp9–pRNALS10 by WT nsp12, the NiRAN mutant (D218A) or the polymerase mutant (D760A). VCE was used as a control but was incubated with [α-32P]GTP. The reaction products were resolved using urea–PAGE and visualized by toluidine blue O staining (top) and autoradiography (bottom). The results in this figure are representative of at least two independent experiments. nt, nucleotides.