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. 2017 Aug 30;45(20):11700–11710. doi: 10.1093/nar/gkx775

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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 4. — PP32 and SET/TAF-Iβ proteins block HAT1 mediated H4 acetylation in vitro. Acetylation assay performed using 0.128 nmol of recombinant histone H4 and purified HAT1 in the presence or absence of increasing amounts of recombinant PP32 (A) and recombinant SET/TAF-Iβ (B), followed by H4K12ac Dot-blot detection. Top: graph of the remaining HAT1 activity. 100% activity correspond to the HAT1 mediated H4 acetylation in the absence of PP32 and SET/TAF-Iβ. Bottom: a representative H4K12ac dot blot HAT1 assay. FT corresponds to the flow through material of the recombinant SET/TAF-Iβ Ni⁺²-beads purification. (C) Top: Coomassie blue stained gel of the different recombinant proteins used in the acetylation assay. Bottom: acetylation assay performed as in (A), pre-incubating H4 as indicated. (D) Acetylation assay performed using recombinant histone H4 and purified HAT1 in the presence of 8 pmol of recombinant PP32, 12 pmol of recombinant SET/TAF-Iβ, and a mix of 8 pmol of recombinant PP32 and 12 pmol of recombinant SET/TAF-Iβ (Mix 1×), and 4 pmol of recombinant PP32 and 6 pmol of recombinant SET/TAF-Iβ (Mix 0.5×).