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. 2018 Feb 23;9:799. doi: 10.1038/s41467-018-03148-5

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© The Author(s) 2018

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. 4 — ZUFSP UBDs contribute to chain cleavage and specificity. a Schematic representation of ZUFSP domain architecture. UBZ-like zinc fingers (Z), MIU domain (M), novel ZUFSP ubiquitin-binding domain (zUBD) and α2/α3 region are shown as boxes. b Activity of ZUFSP FL and truncations lacking the UBDs against K63-linked Ub₆₊ chains. Positions of the truncated ZUFSP proteins are indicated by arrows. c Comparison of Mug105 and ZUFSP^310-578 activity against ubiquitin-AMC. The shown RFU values are the mean of triplicates. d Chain specificity of ZUFSP catalytic core (ZUFSP^310-578) compared to full-length Mug105. Both DUBs were tested against K48- and K63-linked Ub₂ for the indicated time points. e Pull-down analysis of ZUFSP (full-length and two N-terminal truncations) against a mixture of K63-linked Ub₄ and Ub₅ chains