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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 interacts with NF-κB Rel, and the LXXLL motif in bPIAS is not required for binding and inhibiting bRel. (a,b) Co-IP analyses of the interactions between bPIAS and bRel (a) or bIκB (b). (c) The bPIAS-(LL-AA) point mutants used in this study. (d) Co-IP assays indicate that the bPIAS-AA point mutant is also capable of binding to bRel, similar to its wild-type counterpart. (e) Luciferase reporter assays show that bPIAS-AA can inhibit bRel-dependent transcription activation to the same extent as the wild-type bPIAS. (f) Western blot was performed to show the expression of relevant proteins, including bPIAS-WT, bPIAS-AA and bRel, β-actin was used as the internal reference. (g) Co-IP assays indicate that the hsPIAS3-AA point mutant is also capable of binding to hsp65, similar to its wild-type counterpart. (h) Luciferase reporter assays show that hsPIAS3-AA can inhibit hsp65-dependent transcription activation to the same extent as the wild-type hsPIAS3. Data show a representative result from at least three separate experiments. ^*P < 0.05, ^**P < 0.01, ^***P < 0.001.