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. 2017 Dec 6;7:17063. doi: 10.1038/s41598-017-16624-7

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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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Amphioxus PIAS blocks the DNA binding ability of NF-κB Rel. (a) Domain structures and various truncated variants of bRel used in this study. (b) Co-IP analyses of the interactions between bPIAS and the truncated mutants of bRel. (c,d) Luciferase reporter assays were performed in HEK293T cells with an expression construct encoding Gal4-bRel fusion protein, increasing amounts of bPIAS, and either 2 × NF-κB reporter (c) or 5 × Gal4 reporter (d). (e) Co-IP analyses of the interactions between the truncated mutants of bPIAS and bRel. All experiments were conducted at least twice. All reporter assays were performed in triplicate and repeated at least twice. Values are expressed as the mean ± SD; ^*P < 0.05, ^**P < 0.01, ^***P < 0.001.