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. 2020 Jul 1;10:10755. doi: 10.1038/s41598-020-67549-7

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© The Author(s) 2020

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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DBD of Nurr1 bound to the NBRE-motif located in the second intron of the RasGRP1 gene. (A) SDS–PAGE gel stained with Coomassie brilliant blue, showing the affinity purification of the recombinant Nurr1 protein used for the electrophoretic mobility shift assay (EMSA). (B) EMSA for testing the binding ability of the NBRE-motif containing DNA and the DBD of the purified recombinant Nurr1. Biotin-labeled DNA probe (25 ng) was incubated with purified recombinant GST and GST-DBD (3.75 μg), and the DNA–protein complexes were separated on 6% native polyacrylamide gels. (C) The specific binding ability of the DBD of the Nurr1 protein and NBRE-motif containing probe of the RasGRP1 gene was analyzed by competition assay using non-labeled oligonucleotide (2,000 ng). Non-labeled probe (2000 ng) and biotin-labeled DNA probe (25 ng) from the promoters were incubated with purified recombinant GST and GST-DBD (3.75 μg), and the DNA–protein complexes were separated on 6% native polyacrylamide gels. These experiments were repeated three times.