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. 2018 Oct 2;8:14689. doi: 10.1038/s41598-018-32942-w

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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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The Tet1-SID binds to the PAH1 domain of Sin3A. (A) Schematic diagram showing the boundaries of Sin3A deletion constructs and relevant domains, PAH domains 1, 2, 3 and 4 are indicated by boxes. PAH4 is shaded in grey as it is likely non-functional. HID – HDAC interaction domain. Lower panel, GST-pulldown with the SID domains of Sap25 and Tet1 using ³⁵S-Met using the indicated Sin3A truncations. Short and long exposures of the gel were taken to visualize the binding of Tet1 to PAH1 as indicated. (B) GST-pulldown experiment using the indicated GST-fusion proteins with ³⁵S-Met labelled full-length Sin3A. (C) GST-pulldown with GST-Tet1 and full-length ³⁵S-Met labelled Sin3A. Mutations in individual PAH domains (P1–P4) to either Proline (PP) or Alanine (AA) are indicated. This image is cropped, the uncropped version of the gel is shown in Supplementary Fig. S5B. (D) GST-pulldown with GST-PAH domains (1–3) and Tet1 746–951 labelled with ³⁵S-Met.