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. 2024 Sep 1;15:7608. doi: 10.1038/s41467-024-51962-x

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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. 5 — a IPI7 is required for K29-polyubiquitination of IPA1. The assay was performed in wild-type plants and ipi7-ko plants. Immunoprecipitation was performed with an IPA1 antibody and immunoblotting was performed with an antibody against IPA1, Ub or K29-polyubiquitin chain (K29). Proteins before immunoprecipitation (input) were detected with an antibody against actin for normalization. Effects of M. oryzae infection on the ubiquitination of IPA1 in vivo in wild-type (b) and ipi7-ko (c) plants. Leaves were collected after inoculation with (+) or without (−) M. oryzae. Immunoprecipitation was performed with an IPA1 antibody and immunoblotting was performed with an antibody against IPA1, Ub or K29. Proteins before immunoprecipitation (input) were probed with an antibody against actin for normalization. Similar results were obtained from three independent biological experiments in the datasets.