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. 2017 Aug 11;7:7867. doi: 10.1038/s41598-017-08384-1

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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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EMSA assays showing direct binding of NRF1 and ZSCAN10 to the SIX1 promoter in vitro. (a) Sequence and putative transcription factor-binding sites in the wild type (WT) and mutation type (MT) in the proximal minimal promoter of SIX1 gene. The putative transcription factor binding sites are boxed. The primers for the unidirectional deletions are underlined. (b) Nuclear protein extracts were incubated with a free probe containing the NRF1 binding site in the presence or absence of any competition (lane 2), 50× mutation probe (lane 3) and 50× unlabelled probe (lane 4). The super-shift assay was conducted using 10 μg anti-NRF1 antibodies (lane 5). (c) Nuclear protein extracts were incubated with a free probe containing the ZSCAN10 binding site in the presence or absence of any competition (lane 2), 25× mutation probe (lane 3) and 25× unlabelled probe (lane 4). The super-shift assay was conducted using 10 μg anti-ZSCAN10 antibodies (lane 5). The arrows mark the main complexes.