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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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Identification of binding interfaces of GRLBDm· HSP-90·PPH-5/FKB-6 complexes derived from XL-MS. (A) Crosslinked protein complexes with composition as indicated in the figure were analysed by SDS-PAGE. Binary or ternary complex representing bands, as highlighted by the frame, were excised and analysed by mass spectrometry. The uncut gel image is shown in Supplementary Fig. S1. (B) Schematic representation of the inter-protein crosslinked products detected between HSP-90, GRLBDm and PPH-5. Lines represent the contacts between the two proteins and the chaperone whereas asterisks represent the crosslinked products detected between PPH-5 and GRLBDm. (C) Schematic representation of the inter-protein crosslinked products detected between HSP-90, GRLBDm and FKB-6. (D) Schematic representation of the full length and truncated FKB-6 variants. E) Domain specific binding of FKB-6 and FKB-6 deletion constructs to GR-LBDm·HSP-90 analysed by sedimentation velocity AUC.