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. 2021 Apr 30;220(7):e202005130. doi: 10.1083/jcb.202005130

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© 2021 Su et al.

This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).

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Figure S2. — Recombinant Sgo1 was successfully purified and maximum Sgo1 SUMOylation required the coiled-coil domain. (A) Purification of Sgo1. Coomassie staining confirmed the successful purification of wild-type and Sgo1-4R proteins. (B) Schematics describing the truncation mutants generated for Sgo1. The conserved coiled-coil and basic domains are highlighted in red and blue, respectively. Results from C and D are summarized on the right. (C) The first 208 amino acids are essential for Sgo1 SUMOylation. In vivo SUMOylation was assessed for the following Sgo1-6HA tagged strains as described in Fig. 2 A, together with the indicated negative controls: wild type (AMy7654), sgo1Δ2-108 (AMy14764), sgo1Δ 2–208 (AMy14765), and sgo1Δ2-308 (AMy14766). Unmodified Sgo1 bands are marked with asterisks. IB, immunoblot. (D) The coiled-coil domain is required for maximum Sgo1 SUMOylation. In vivo SUMOylation was assessed for the following Sgo1-6HA tagged strains: wild type (AMy7654) and sgo1Δ2-40 (AMy18194).