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. 2019 Jan 30;9:948. doi: 10.1038/s41598-018-37442-5

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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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β-catenin interacts with the chromatin repressive complex. (a) Table showing genomic annotation of common ERVs bound by β-catenin and KAP1 in BJ1 (columns 2, 3), and among β-catenin, KAP1 in BJ1 and KAP1 in JB1 mESCs (columns 4, 5), represented as number (#) and percentage (%) over the total common peaks. (b) Quantitative real-time PCR experiments showing the expression profiles of ERVs (IAP, MusD, MERVL) in E14 (upper charts) and GS1 (lower charts) YP- and OP- mESCs. The transcriptional levels are normalized to Gapdh as a reference gene. Data are represented as fold change (2^−ΔΔCt) relative to the YP-mESCs and the results are means of n = 3 independent experiments ± SE. (c) ChIP-qPCR analysis of H3K9me3 recruitment at IAP, MusD and MERVL ERVs in E14 (upper charts) and GS1 (lower charts) YP- and OP- mESCs. The data are represented as fold change (2^−ΔΔCt) over H3 and means of n = 3 independent experiments ± SE. (b,c) Asterisks indicate statistical significance calculated by unpaired two-tailed t test analysis (n.s. not significant; *p < 0.05; **p < 0.01). (d) Co-immunoprecipitation of β-catenin with either KAP1 or DNMT1 followed by western-blot analysis, in shCtrl -or shβcat- transduced E14 mESCs. 10% of input was used for DNMT1, KAP1 and β-catenin IP. IgG were used as negative control. An empty well was included between each experimental condition (Input, IgG and IP) to avoid cross-contamination.