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. 2019 Aug 9;60:16. doi: 10.1186/s40529-019-0264-z

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© The Author(s) 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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.

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Fig. 4 — ABF3 and 14-3-3ω protein–protein interactions are revealed using bimolecular fluorescence complementation (BiFC). The 14-3-3ω, Di19-2, ACS7, ABF3 proteins were paired with empty vectors used as negative controls. The interaction between YFP^N-Di19-2 and YFP^C-14-3-3ω/YFP^C-Di19-2 and YFP^N-14-3-3ω/YFP^N-ACS7 and YFP^C-14-3-3ω/YFP^C-ACS7 and YFP^N-14-3-3ω was localized to the nucleus and cytosol as shown in the confocal microscopy images. DAPI was used to stain the nucleus. ACS7 interacts with 14-3-3, and therefore, was introduced as a positive control (Huang et al. 2013). BiFC experiments showed an interaction between ABF3 and 14-3-3ω in Arabidopsis protoplasts. Point mutations of ABF3 (T451A) abolished its interaction with 14-3-3ω. DAPI was used to stain the nucleus