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. 2023 May 30;14:3126. doi: 10.1038/s41467-023-38404-w

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© The Author(s) 2023

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. 7 — a Cryo-EM structure of the rat 20S proteasome/CBR3 complex. A prominent extra density is displayed at the β-ring region. b Atomic model of the 20S proteasome structure (PDB:6TU3) (cyan) was fitted into the electron density map. The extra electron density near the PSMB4 subunit (magenta) reveals the binding site of CBR3. c Escherichia coli cell lysates overexpressing FLAG-tagged human β-subunits PSMB1 to PSMB7 were incubated with His₆-CBR3 bound to Ni-beads for pull-down experiments. Bound subunits were detected using an anti-FLAG antibody. d Densitometry quantification indicated that the pull-down of PSMB4 greatly exceeds the levels of the other β-subunits. The bar graph shows the average values of each PSMB subunit intensities in the pull-down, normalized to the corresponding lysate, from three independent replicates; each replica is color-coded (red, green, and blue). Error bars represent SEM. Significance was calculated using one-way ANOVA (p-value = 0.0309), with Dunnett’s post-hoc test (* represents p-value = 0.0145, 0.0168, 0.0163, 0.0191 for the significances between PSMB4 and PSMB1, PSMB3, PSMB5, and PSMB7, respectively). Source data are provided with this paper.