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. 2023 Jul 3;193(2):1161–1176. doi: 10.1093/plphys/kiad385

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© The Author(s) 2023. Published by Oxford University Press on behalf of American Society of Plant Biologists.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 6. — TgbHLH95 protein interacts with TgbZIP44. A) BiFC analysis of the interaction between TgbHLH95 and TgbZIP44. The pairs of fusion proteins tested were TgbHLH95-YFP^N + TgbZIP44-YFP^C and TgbZIP44-YFP^N + TgbHLH95-YFP^C. PHR2-Y^N and SPX4-Y^C were used as the positive control; YFP^N and YFP^C were used as negative controls. Nuclear location signal (NLS) indicates the position of the nucleus. Scale bars = 50 µm. B) LCI analysis of the interaction between TgbHLH95 and TgbZIP44. Tobacco leaves were infiltrated with Agrobacterium strain GV3101 harboring different constructs. The luminescence signals of the infiltrated areas were measured 48 h after infiltration. The experiment was repeated at least 3 times. C) Co-IP assay of TgbHLH95 and TgbZIP44. TgbHLH95-Flag plus TgbZIP44-GFP proteins were immunoprecipitated with an anti-GFP antibody and immunoblotted with anti-GFP and anti-Flag antibodies. D) Pull-down assay detection of the interaction of TgbHLH95 and TgbZIP44. The recombinant TgbHLH95-GST or GST was incubated with TgbZIP44-His. Blots were probed with anti-GST and anti-His antibody.