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. 2018 Feb 16;8:3155. doi: 10.1038/s41598-018-21194-3

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© The Author(s) 2018

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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Preferential binding of Twist1/E12 or Twist1/E47 to E2 and E5. Double-stranded synthetic oligonucleotides containing the E-box were end-labelled with biotin and used as a probe for EMSA. The oligonucleotides sequences used in EMSA (E1E2, E1M2, M1E2, and E5) are shown in Table 2. Results shown in (a) and (b) are from assays using the oligonucleotides containing the consensus E-box sequences (E1E2 and E5) and mutated oligonucleotides (E1M2, M1E2, and M5), respectively. Biotin-labelled probes were incubated with nuclear extracts from HEK293T cells transfected with the empty vector pcDNA3 as a control, or expression vectors encoding the FLAG fusion of human E12 (fhE12), mouse E12 (fmE12), mouse E47 (fmE47), and mouse Twist1 (fmTwi). Binding reactions were performed in the presence or absence of non-labelled oligonucleotides as binding competitors (Comp) or an anti-FLAG antibody (Ab). The positions of shifted and super-shifted bands are shown with black and hollowed arrowheads, respectively.