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. 2017 Jun 27;45(16):9388–9397. doi: 10.1093/nar/gkx563

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© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 7. — Esco2 acetylates histone H4 at Lys16 in vitro. (A) Flag purification of Esco2. Esco2 and enzymatically mutant Esco2-W530G were expressed in HEK293 cells and then purified according to the Flag purification procedure. Purified Esco2-Flag and Esco2-W530G-Flag were detected with sodium dodecyl sulphate-polyacrylamide gel electrophoresis followed by both coomassie staining and western blotting with anti-Esco2 antibody. (B) Commercially obtained recombinant histone H4 was identified by both coomassie staining and western blotting with anti-H4 antibody. (C) In vitro acetylation assay with Esco2-Flag. Recombinant histone H4 was incubated with or without purified Esco2-Flag and Ac-CoA in the acetyltransferase assay buffer at 30°C for 1 h. The reactions were analyzed by western blotting with anti-histone H4 (acetyl K16) antibody for acetylation levels of H4K16 and anti-histone H4 antibody as a loading control. (D) In vitro acetylation assay with Esco2-W530G-Flag. Recombinant histone H4 was incubated with or without purified Esco2-W530G-Flag and Ac-CoA in the acetyltransferase assay buffer at 30°C for 1 h. The reactions were analyzed by western blotting with anti-histone H4 (acetyl K16) antibody for acetylation levels of H4K16 and anti-histone H4 antibody as a loading control.