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. 2020 Aug 19;48(16):9250–9261. doi: 10.1093/nar/gkaa684

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© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 2. — METTL4 directly catalyzes m⁶Am formation in vitro. (A) Western blotting of cell lysate from Mettl4-KO HEK293T transfected with METTL4^WT or METTL4^CD or untransfected (control). Expected size of purified protein is 57kDa. HSP60 (∼61 kDa) is displayed as a comparison. (B) Sequence of U2-Am30 and U2-A30 RNA substrates used for in vitro methylation. ‘AAG’ sites are highlighted in red. (C) Anti-m⁶A dot blotting of RNA substrates in vitro methylated by METTL4^WT or METTL4^CD. Duplicate dots are shown. (D) Nucleoside HPLC–MS/MS of m⁶Am as a percentage of total m⁶Am and Am in RNA substrates in vitro methylated by METTL4^WT or METTL4^CD. Displayed are average and standard deviation error of triplicates. One-tailed Student's t-test P-value is shown.