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. 2020 Mar 9;11:1276. doi: 10.1038/s41467-020-14942-5

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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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Fig. 2 — a Top panel: BioLayer Interferometry (BLI) experimental approach. Bottom panel, binding layer thickness on probe normalized to baseline. Probes were loaded with oligos containing the SRTF1 binding site (red line) or a scrambled sequence (gray line). Addition of progesterone resulted in rapid unbinding of SRTF1 (red line) that was not observed with vehicle control (cyan line). b Unbinding of SRTF1 is dose-responsive. Dissociation curves in duplicate were normalized such that binding at time 0 was equal to 1. c Fraction SRTF1:DNA complex from curves shown in panel b dissociated at 5 s. d Dissociation curves in triplicate of SRTF1 in the presence of 5 μM various steroids showing strongest induction by progesterone normalized as in panel b. e Fraction SRTF1:DNA complex from curves shown in panel d dissociated at 30 s. Error bars are standard error over three experiments. Data underlying bar graphs in panels c and e are available in the Source Data file.