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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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The Hsp104 N domain is bipartite and mediates both substrate binding and Hsp70 interaction. (a) Key residues involved in substrate binding are shown in red (Set-1), and those involved in Hsp70 interaction²¹ in blue (Set-2). (b,c) Set-1 and Set-2 mutants affect protein disaggregation differently. Disaggregase activities of Hsp104 and Hsp104 variants (Set-1 red; and Set-2 blue) in the presence of Hsp70/40. Recoveries of (b) FFL and (c) G6PDH activity expressed relative to the native bi-chaperone system. (d,e) Set-1_T4L and Set-2_T4L show substantial defects in protein disaggregation in a constitutively active background. (d) Impaired recovery of β-gal activity by Set-1_T4L (red) and Set-2_T4L (blue). (e) Hsp70/40 restores the protein disaggregation defect of Set-1_T4L (red), but not of Set-2_T4L (blue). Averages of three independent measurements ± SD are shown.