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. 2020 Jul 1;10:10733. doi: 10.1038/s41598-020-67645-8

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© The Author(s) 2020

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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Hormone binding to GRLBDm is modulated by HSP-90, ATP and TPR-cofactors. (A) Association kinetics of F-DEX tο GRLBDm (grey) in the presence of C. elegans HSP-90 (red) and nucleotides as indicated in the plot. (B) Sedimentation velocity analysis of F-DEX bound to GRLBDm (grey) in the presence of C. elegans HSP-90 (red) and nucleotides as indicated in the plot. (C) Association kinetics of F-DEX tο GRLBDm (grey) in the presence of C. elegans HSP-90/ATP (red) and cofactors as indicated in the plot. (D) Sedimentation velocity analysis of F-DEX bound to GRLBDm (grey) in the presence of C. elegans HSP-90/ATP (red) and cofactors as indicated in the plot. (E) Influence of TPR-cofactors on the hormone-binding rates of GRLBDm as determined from fluorescence polarization kinetics. All samples contained HSP-90 and ATP plus the indicated cofactors. Statistical significance was assessed by a two-sample t-test and a level of significance of 0.05. Error bars represent the standard deviation of three independent measurements (n = 3).