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. 2017 Jul 10;7:5026. doi: 10.1038/s41598-017-04913-0

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© The Author(s) 2017

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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Interaction analysis of chickpea CaMAPKs with CaTCP transcription factors. (A) Y2H analysis of chickpea CaMAPKs with CaTCPs. Three members of class I TCP transcription factors from chickpea were fused with Cub-LexA-VP16 in pGDHB1vector and transformed in yeast strain NMY51. Chickpea MAPKs were fused with mNub in pGPR3-N vector and transformed in yeast strain NMY61. After mating and two round of selection, the yeast cells were spotted on SD/-L-W and SD/-L-W-H-A plates. Plates were photographed after 48 h growth and X-gal overlay assay was performed to check the activation of LacZ gene as third reporter. Yeast growth on SD/-L-W-H-A and blue colour after X-gal overlay assay suggests protein-protein interaction. (B) BiFC assay of five CaMAPKs and one CaTCP encoded by LOC101493313. Independently five CaMAPKs were tagged with C-terminal half of YFP and CaTCP was tagged with N-terminal half of YFP. Plasmid DNA of a CaMAPK and CaTCP pair was precipitated on 1 µm gold particles and bombarded on onion epidermal cells. The cells were observed under confocal microscope after 48 hours. In all five, YFP signal was visualised in nucleus. Scale bars, 50 µm.