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. 2019 Apr 19;9:6304. doi: 10.1038/s41598-019-41684-2

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© The Author(s) 2019

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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The intermediate domain of GFI1 interacts with the C-terminal domain of p53 (A) 293T cells were transfected with vectors expressing variants of the GFI1-Flag-HA fusion protein. Nuclear extracts from these proteins were immunoprecipitated for Flag, separated by SDS-PAGE and blotted for the indicated proteins. Blots from input controls are shown below. (B) Schematic representation of the variant GFI1 proteins used in (A). (C) 293T cells were transfected with vectors expressing variants of the p53-HA fusion protein as well as GFI1-Flag protein without an HA tag. Extracts were immunoprecipitated for HA and blotted for the indicated proteins. (D) Schematic representation of the variant p53 proteins used in (C). (E) Proposed model of the interaction between GFI1 and p53. (F) GFI1-Flag-HA fusion protein was immunoprecipitated in 293T cells in the presence or absence of ethidium bromide and blotted for p53. (G) GFI1-Flag-HA fusion protein was immunoprecipitated in 293T cells in the presence or absence of benzonase and blotted for p53.