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. 2017 Aug 30;7:10084. doi: 10.1038/s41598-017-10935-5

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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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Aurora A phosphorylates YY1 in vitro in its DNA-binding domain. (a) Radioactive in vitro kinase assay using bacterially-expressed and purified YY1 with active Aurora A kinase. After completion, the reactions were separated by SDS-PAGE electrophoresis. The gel was stained with Coomassie blue, dried, and then exposed to a phosphor-imager screen to detect the radioactive phospho-labelling on YY1. (b) Radioactive kinase assay as in (a) but using bacterially expressed and purified GST or GST-YY1 full-length or deletion mutants as substrates for Aurora A phosphorylation. (c) Schematic illustration of the YY1 full length and deletion mutants used in (b). The presence or absence of Aurora A phosphorylation is indicated to the right. The structural and functional domains of YY1 are labelled on the top^{33, 34}.