Extended Data Fig. 7: Identification of a conserved alanine residue in the N-terminal region of METTL3 required for its interaction with eIF3h.

a, Secondary structure prediction of the N-terminal (1–200) region of METTL3 protein showing putative alpha helices (blue lines). b, Evolutionary conservation of the N-terminal (1–200) region METTL3 protein. c, Computational modelling of the 3D structure of the N-terminal (77–163) region METTL3 protein, on the basis of the coordinates of RCSB Protein Data Bank entry 3HHH. d, Western blotting using the indicated antibodies. The blot is representative of two independently performed experiments with similar results. e, RT–qPCR analysis of reporter mRNAs. FLuc–MS2bs mRNA levels were normalized to RLuc mRNAs. The FLuc:RLuc ratio obtained in Flag–MS2 (control) was set to 1. Data are mean ± s.d. from six independent experiments. f, Immunoprecipitation of Flag–METTL3 (wild-type or METTL3(A155P)) and western blotting analysis using the indicated antibodies. Blots are representative of two independently performed experiments with similar results. g, Staining of recombinant protein wild-type His–Flag–MS2–METTL3 or His–Flag–MS2–METTL3(A155P). Gel is representative of two independently performed experiments with similar results.