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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. 4 — The indicated HMA domains of RGA5 (wild type, m1, and m1m2) and Pikp-1, fused to YFP, were transiently co-expressed in N. benthamiana leaves with HA-tagged AVR-Pia, AVR-PikD, and AVR-PikC (without signal peptides). Proteins were extracted after 48 h, separated by gel electrophoresis, and tagged proteins were detected in the extract (input) and after immunoprecipitation with anti-GFP beads (IP-GFP, trapping YFP fusions) 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 experiment was carried out twice with similar results.