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. 2021 Jan 6;14:4. doi: 10.1186/s12284-020-00451-y

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© The Author(s) 2021

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 — OsMS188 interacts with TDR. a Amino acid sequence alignment of OsMS188 and AtMS188. The red box indicates the activation domain and the red dots indicate the number of OsMS188 amino acid sequences. b Identification of the activation domain of OsMS188. The full-length CDS of OsMS188 allowed growth on selective media lacking Leu, His and adenine. The yeast could not grow on selective media when the last 14 amino acids were deleted. c Yeast two-hybrid (Y2H) assay showing the physical interaction of OsMS188 with TDR. The OsMS188 CDS without the self-activation fragment (OsMS188ΔC) was fused to the DNA-binding domain (BD) in pGBKT7, and the TDR CDS was fused to the GAL4 activation domain (AD) in pGADT7. The interactions are indicated by blue-coloured yeast colonies on SD/−Ade/−His/−Trp/−Leu/X-a-Gal media. d LCI assay showing the interaction between OsMS188 and TDR. Fluorescence signal intensities indicate interaction activities