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. 2020 Aug 28;19(2):300–310. doi: 10.1111/pbi.13462

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© 2020 The Authors. Plant Biotechnology Journal published by Society for Experimental Biology and The Association of Applied Biologists and John Wiley & Sons Ltd.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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OsRE1 physically interacts with OsRIP1. (a) Yeast two‐hybrid assay showed that OsRE1 interacts with OsRIP1. Yeast was grown at 30 °C for 3 days. Empty vectors were used as the negative controls. AD, activation domain. BD, binding domain. (b) In vitro pull‐down assay showed that OsRE1‐His pulls down MBP‐OsRIP1 but not free MBP. Free MBP and His resin were used as the negative controls. (c) Bimolecular fluorescence complementation (BiFC) assays showed OsRE1 interacts with OsRIP1 in nucleus (labelled by fluorescence of 4′, 6‐diamino‐2‐phenylindole) in leaf epidermal cells of N. benthamiana. Scale bars, 20 μm. (d) In vivo Co‐IP assay showed that Flag‐OsRIP1 can be co‐immunoprecipitated in the total leaf extract N. benthamiana expressing OsRE1‐GFP but not free GFP using anti‐GFP agarose beads. [Colour figure can be viewed at wileyonlinelibrary.com]