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. 2024 Nov 1;15:9448. doi: 10.1038/s41467-024-53894-y

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.

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Fig. 3 — a Interactions between TbCSB βC1 and NbHSP90s in the yeast two-hybrid assay. Yeast AH109 transformed with the indicated plasmid combinations were spotted with 10-fold serial dilutions on synthetic dextrose media SD/-Leu-Trp and SD/-Ade-His-Leu-Trp. b Interaction between TbCSB βC1 and NbHSP90-2 in the co-IP assay. TbCSB βC1-Flag and NbHSP90-2-HA were co-expressed in N. benthamiana leaves, and TbCSB βC1-Flag+GFP-HA served as a negative control. TbCSB βC1-Flag interacting proteins were immunoprecipitated with anti-Flag beads. GFP-HA and NbHSP90-HA proteins were detected with anti-HA antibodies and TbCSB βC1-Flag with anti-Flag antibodies in input samples and after co-IP. c Interaction between TbCSB βC1 and NbHSP90-10 in co-IP assay. TbCSB βC1-Flag and NbHSP90-10-HA were co-expressed, and TbCSB βC1-Flag+GFP-HA served as a negative control. Source data are provided in Source Data file.