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. 2022 Mar 21;13:1524. doi: 10.1038/s41467-022-29196-6

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© The Author(s) 2022

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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Fig. 2 — Interaction of AVR-PikD, AVR1-CO39, and AVR-PikD (without signal peptides and fused to the DNA binding domain (BD) of the GAL4 transcription factor) with the HMA (residues 991–1072) and C-terminal (residues 883–1116) domains of RGA5 and variants carrying mutations designed to introduce the AVR-PikD-binding surface (fused to GAL4 activation domain (AD)) was assayed by yeast two-hybrid experiments. The HMA domain of Pikp-1 (AD:HMA_Pikp-1) and the AD and BD domains alone were used as controls. Four dilutions of diploid yeast clones (1/1, 1/10, 1/100, 1/1000) were spotted on synthetic TDO medium (-Trp/-Leu/-His) supplemented with 0.5 mM and 10 mM of 3-amino-1,2,4-triazole (3AT) to assay for interactions and on synthetic DDO (-Trp/-Leu) to monitor proper growth. Pictures were taken after 5 days of growth.