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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 functions as a histone decrotonylase whose activity is modulated by inositol phosphates. Deacetylase and decrotonylase activities were measured using a Caliper assay with continuous substrate turnover for a 60 min period. Analogous H3K18ac (A), H3K18cr (B) and H4K16ac (C) fluorescein-tagged peptides were incubated with recombinant HDAC1/CoREST1/LSD1 ternary complex. Graphs show the average percentage conversion (mean ± SD; n = 2), initial rates and percentage conversion of substrate at the end point ±100 μM InsP₆ (D-myo-inositol 1, 2, 3, 4, 5, 6-hexakisphosphate).