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. 2017 Oct 9;7:12849. doi: 10.1038/s41598-017-12924-0

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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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HBZ inhibits the DNA-binding activity of NRF-1 by physical interaction with NRF-1. (A) HBZ reduces NRF-1 binding to the NRF-1-binding motif in the TDP1 promoter. A gel-shift assay was used to analyze protein-DNA interactions. HEK293T cells were transfected with increasing amounts of HBZ (0, 1, 2, and 4 µg). Expression of NRF-1 and HBZ protein contained in the nuclear extracts was analyzed by immunoblotting. The position of the relevant protein-DNA complexes is indicated by the arrow. (B) Jurkat T cells and Jurkat-HBZ cells were immunoprecipitated with anti-NRF-1 antibody and quantified by real-time PCR. Data shown are the mean ± SD (n = 3). (C) Schema of HBZ gene. (D) Schema of NRF-1 gene. (E) and (F) The expression vectors of the indicated proteins were co-transfected into HEK293T cells, and their interactions were analyzed by co-immunoprecipitation assay. (G) NRF-1 was purified from E. coli as a GST fusion protein. GST alone or GST-NRF-1 was incubated with in vitro transcribed/translated HBZ-mycHis. GST pull-downs and input were subjected to Western blotting with anti-Myc antibody.