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. 2018 Oct 2;8:14690. doi: 10.1038/s41598-018-32927-9

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© The Author(s) 2018

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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HDAC1/2 are the dominant histone decrotonylases in ES cells. (A) The decrotonylase activity of HDAC1/2 complexes isolated from ES cells, using antisera to HDAC2 and LSD1, were measured using a Boc-Lys(Cr)-AMC substrate. No cell lysate (neg) and normal mouse IgG were used as negative controls. Average (±SD) plots of n = 3 technical replicates. (B) Quantitative western blot data for the indicated proteins in Ctrl (day 0) and DKO ES cells treated with 4-hydroxytamoxifen (OHT) at day 3, were performed using an Odyssey scanner. Graphs show the average normalized signal intensity (mean ± SEM; n ≥ 3) relative to Histone H3. Uncropped scans of western blots are shown in Supplementary Fig. 3A–C. (C) Deacetylase and (D) decrotonylase assays were performed using whole-cell extracts from Ctrl (day 0) and DKO ES cells (day 3, following OHT treatment). Average (±SD) plots of n = 3 technical replicates. (E) Changes in both deacetylase and decrotonylase activity in DKO ESCs were calculated as a percentage of CTRL ES cells from the values depicted in (C) and (D).