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. 2022 Mar 31;50(7):4012–4028. doi: 10.1093/nar/gkac184

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© The Author(s) 2022. 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-NonCommercial License (https://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 3. — METTL8-Iso1 forms polymers. (A) SDS–PAGE analyses of purified recombinant mature METTL8-Iso1 and METTL8-Iso4 from the E. coli expression system. (B) Gel filtration analysis of purified mature METTL8-Iso1. (C) Determination of the molecular mass of mature METTL8-Iso1 and METTL8-Iso4 based on the elution volumes of four protein standards, namely, apoferritin (443 kDa), yeast alcohol dehydrogenase (150 kDa), bovine serum albumin (66 kDa) and carbonic anhydrase (29 kDa). (D) The METTL8-Iso1-FLAG and METTL8-Iso1-EGFP genes were coexpressed in HEK293T cells. METTL8-Iso1-EGFP was precipitated by METTL8-Iso1-FLAG in a co-IP assay.