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. 2019 Apr 5;9:5691. doi: 10.1038/s41598-019-42177-y

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© The Author(s) 2019

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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TaJAZ1 physically interacts with TaNINJA. (a) LCI assay showing the interaction between TaJAZ1 and TaNINJA. EV were used as negative controls. (b) BiFC assay illustrating the TaJAZ1-TaNINJA interaction in the nucleus of N. benthamiana leaf cells. TaJAZ1 and TaNINJA were separately fused with the N- and C-terminal part of YFP (nYFP and cYFP). YFP fluorescence was detected 48 h after infiltration. Bars = 20 µm. (c) Schematic representations of the domain structures of TaNINJA and truncated versions of TaNINJA proteins. (d) LCI assay illustrating that C-terminus of TaNINJA mediates its interaction with TaJAZ1. The nLUC and cLUC EVs were used as negative controls. (e) Mapping of the interaction domain of TaJAZ1 with TaNINJA. The signals of the interaction were collected 48 h after infiltration. Eight N. benthamiana leaves were analyzed in each experiment and similar results were observed.