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. 2023 Jun 20;23:327. doi: 10.1186/s12870-023-04294-9

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© The Author(s) 2023

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 10 — Physical interaction between VQs. A Transcriptional activation validation assays. B Yeast-two-hybrid assays. ClVQ12, ClVQ4, and ClVQ26 can interact with each other. Sequences of full-length ClVQ4, ClVQ12 and ClVQ26 were fused to the pGBKT7 binding domain (BD, bait), sequences of full-length ClVQ4 Aand ClVQ12 were fused to the pGADT7 activation domain (AD, prey)