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. 2017 Sep 11;7:11184. doi: 10.1038/s41598-017-11474-9

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© The Author(s) 2017

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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Addition of the I116A mutation to Set-1 and Set-2 triple mutants abrogates protein disaggregation. (a) Ribbon diagram of the Set-1_I116A and Set-2_I116A mutants with Ile116 shown in pink. (b) Recovery of β-gal activity by Set-1 and Set-1_I116A (red bars), and Set-2 and Set-2_I116A (blue bars). (c,d) Neither Set-1_T4L/I116A (red bars) nor Set-2_T4L/I116A (blue bars) promotes protein disaggregation without (c) or with Hsp70/40 (d). Averages of three independent measurements ± SD are shown in Fig. 6b–d. (e) The Set-1_N/I116A and Set-2_N/I116A quadruple mutants have reduced protein stability. Thermal shift assay with the isolated N domain (Hsp104_N, grey curve) and its Set-1 (Set-1_N/I116A, red curve) and Set2 variants (Set-2_N/I116A, blue curve). Representative curves from three independent measurements together with the calculated T _m values are shown.