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. 2022 Aug 29;15:46. doi: 10.1186/s12284-022-00592-2

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. 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/4.0/.

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Fig. 6 — OsSKL2 interacts with OsASR1. A OsSKL2 was found to interact with OsASR1 in a yeast two-hybrid system, using BD-OsSKL2 + AD, AD-OsASR1 + BD as negative controls. Growth on selective QDO plates indicated a positive interaction. DDO: yeast SD/-Trp/-Leu selective medium, QDO: yeast SD/-Trp/-Leu/-His/-Ade selective medium. B A pull-down assay was then performed to confirm the interaction between OsSKL2 and OsASR1 in vivo. GST and GST-OsASE1 proteins coupled to beads were incubated with MBP-OsSKL2 fusion proteins. Bound OsSKL2 was then detected using mouse anti-MBP antibody. C A BIFC assay further revealed that OsSKL2 interacts with OsASR1 in rice leaf protoplasts (bar = 10 μm)