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. 2018 Nov 19;9:1675. doi: 10.3389/fpls.2018.01675

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Copyright © 2018 Kim, Jang and Park.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Physical interaction of ORA59 with RAP2.3. (A) Yeast two-hybrid assay. ORA59 with N-terminal 60 amino acids deleted (ORA59Δ1-60) and full-length RAP2.3 were fused with GAL4 AD and BD, respectively. Their interactions were tested on selective media SD/-AHLT and in the presence of X-α-Gal. (B) In vitro GST pull-down assay. GST or ORA59-GST was incubated with RAP2.3-His and precipitated with glutathione sepharose 4B beads. Proteins were detected by immunoblotting with anti-GST and anti-His antibodies. Input shows 1% of the amount used in binding reactions. WB, western blotting. (C) BiFC assay. YFP^NE, YFP^CE, and their fusion proteins bZIP63^NE, bZIP63^CE, ORA59^NE, and RAP2.3^CE were expressed in Arabidopsis protoplasts as indicated. YFP fluorescence signals were visualized under a confocal microscope. Bars, 10 μm. Experiments were repeated three times with similar results.