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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. 6 — RGA5 deleted of its C-terminal domain (RGA5_ΔHMA, residues 1–996) fused to YFP was transiently co-expressed in N. benthamiana leaves with HA-tagged AVR-Pia, AVR-PikD, or PWL2 (without signal peptides). Proteins were extracted after 48 h and tagged proteins were detected in the extract (input) and after immunoprecipitation with anti-GFP beads (IP-GFP) by immunoblotting with anti-HA (α-HA) and anti-GFP (α-GFP) antibodies. Protein loading in the input is shown by Ponceau staining of the large RuBisCO subunit. The HMA domains of Pikp-1 and RGA5 were used as controls as well as the unrelated PWL2 effector of M. oryzae. The experiment was carried out twice with identical results.