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. 2023 Aug 15;9:85. doi: 10.1038/s41421-023-00573-9

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© The Author(s) 2023

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. 5 — a CBB staining showing minimal HDAC1 and HDAC3 core complexes purified from HEK293T cells. The positions of wild-type and mutant HDAC1/3, FLAG-MAT1_162–335, and FLAG-SMRT_350–489 are indicated by white arrows. b In vitro desuccinylation assay for minimal HDAC1 and HDAC3 core complexes prepared from mammalian cells. Approximately 200 ng wild-type or mutant complexes were used for in vitro assay. Histone substrates were prepared from TSA-treated HeLa cells. TSA concentration in in vitro reaction was 10 μM and the reaction time was 2 h. c Dose-dependent histone desuccinylation by purified wild-type HDAC1/FLAG-MAT1_162–335 and HDAC3/FLAG-SMRT_350–489 core complexes. The increasing amount of HDAC1 and HDAC3 core complexes: 100 ng, 200 ng, and 400 ng. d In vitro desuccinylation assay using synthetic H3K14su peptide substrate. Desuccinylation reactions were carried out without or with 200 ng HDAC1 or HDAC3 core complexes as indicated for 2 h. TSA concentration in in vitro reaction was 10 μM.