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. 2020 Oct 30;48(20):11510–11520. doi: 10.1093/nar/gkaa949

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© The Author(s) 2020. 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/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Mimics of lysine acetylation in the H3 tail domain affect H1 CTD condensation. H3 proteins containing K → Q substitutions at known sites of lysine acetylation were incorporated into nucleosomes and the extent of H1 CTD condensation determined by FRET analysis. (A) Schematic showing sites of K → Q substitution in the H3 tail domain. (B–D) FRET analysis of labeled H1 bound to H3 6KQ, H3 3KQ1 and H3 3KQ2 nucleosomes compared to WT at the nucleosome: H1 ratios indicated in the figure legend. NS, no significant difference; (***) P < 0.001, (*) P < 0.05.