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. 2019 Jul 5;10:2999. doi: 10.1038/s41467-019-10850-5

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© The Author(s) 2019

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 — OsSUF4 interacts with SDG725C in vitro and in vivo. a The interaction between OsSUF4 and SDG725C in a yeast two-hybrid assay. AS1 and AS2 serve as the positive control. Upper panel: Schematic representation of full-length and truncated SDG725 proteins. b The left panel showed GST and GST-SDG725C (GST-725C) proteins used in the pulldown assay, and the right panel showed HA-OsSUF4 pulled down by SDG725C using rice plants over-expressing HA-OsSUF4. GST-725C, HA-OsSUF4, and a non-specific band are marked with an asterisk, a triangle, and an open triangle, respectively. c BiFC experiments showing the interaction of OsSUF4 and SDG725C in Nicotiana benthamiana leaf epidermal cells (Bar = 50 µm). DIC differential interference contrast, YN N-terminal of YFP, YC C-terminal of YFP. d Yeast two-hybrid findings that the C-terminal domain of OsSUF4 (OsSUF4C) interacts with SDG725C. Upper panel: Schematic representation of full-length and truncated OsSUF4 proteins. AS1 and AS2 serve as the positive control. Source data are provided as a Source Data file