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. 2022 Jan 20;13:401. doi: 10.1038/s41467-022-28049-6

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© The Author(s) 2022

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. 6 — a–d Activity assays of FL AtZUP or UBZ-truncated AtZUP^64–399 against K48-linked ubiquitin chains (a), K48-linked di-ubiquitin (b), RLRGG-AMC (c), and Ub-PA (d). Arrowheads mark the N- and C-terminal fragments of FL AtZUP (black) or AtZUP^64–399 (green). e, f Activity assays of FL AtZUP and the internal truncations AtZUP^∆219–275, AtZUP^∆243–275 or AtZUP^∆243–268 against K48-linked ubiquitin chains (e) or RLRGG-AMC (f). g Linkage specificity analysis with AtZUP^∆219-275. A panel of di-ubiquitin chains was treated with AtZUP^∆219–275 for the indicated time points. Source data are provided as a Source Data file.