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. 2020 Sep 10;11(9):740. doi: 10.1038/s41419-020-02923-x

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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 — Cell-free ubiquitylation assay of a Recombinant NOXA incubated with recombinant CHIP for indicated time points. b Recombinant CHIP and flag-tagged NOXA incubated with Ub chain-assembly mutants (Kxonly) as indicated. Western blot analysis of cell lysate (Input) and c Strep-PD of HeLa cells transfected with Strep-Ub chain-assembly mutants (Kxonly) for 36 h and treated with 1 µM DOX for 16 h. d Strep-PD of HeLa cells transfected with Strep-Ub chain-assembly mutants (KxR) as indicated for 36 h and treated with 1 µM DOX for 16 h. c, d Actin served as a loading control. e Amino acid sequence of human NOXA harboring one BH3 domain (yellow) and a hydrophobic patch (brown) at the C terminus of the protein. Lysine residues (K) are marked and numbered in red, conserved residues of the BH3 domain are depicted in green and mutated residues are marked with asterisks (3E). NT not transfected. DOX doxorubicin. All experiments are representatives of at least three independent experiments.