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. 2020 Sep 24;29(2):280–288. doi: 10.1038/s41431-020-00728-2

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — NAA10 WT-V5 and NAA10 N101K-V5 were overexpressed in HeLa cells, immunoprecipitated by V5-tag antibody (a) or NAA15 antibody (b) and analysed by Western blotting. Densitometry analysis was performed to quantify NAA10-V5 and NAA15 bands. c Nt-acetylation assay displaying catalytic activity of immunoprecipitated NAA10 WT-V5 and NAA10 N101K-V5. The measured catalytic activity toward NatA substrate SESS₂₄ and monomeric NAA10 substrate EEEI₂₄ was normalised to the amount of immunoprecipitated NAA15 and NAA10-V5, respectively. Reaction mixtures either with immunoprecipitated β-gal-V5 or without peptide were used as negative controls to account for background signal. The IP and activity measurements were performed in three independent setups, each with three technical replicates per assay. One representative setup is shown.