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. Author manuscript; available in PMC: 2019 Apr 25.
Published in final edited form as: Nat Struct Mol Biol. 2018 Aug 27;25(9):841–849. doi: 10.1038/s41594-018-0114-9

Figure 1. The ZZ domain of p300 recognizes histone H3.

Figure 1.

(a) Schematic representation of p300 domain architecture. (b, c) Peptide pull-down assays of the p300 ZZ domain with the indicated histone peptides. Uncropped blot images are shown in Supplementary Data Set 1. (d) Superimposed 1H,15N HSQC spectra of p300-ZZ collected upon titration with H3 peptide (residues 1–12 of H3). Spectra are color coded according to the protein-to-peptide molar ratio. (e) Binding affinities of WT p300-ZZ for the indicated histone peptides measured by tryptophan fluorescence. The experiments were carried out in triplicate for H3 and H3K4ac and in duplicate for methylated H3. (f) Representative binding curve used to determine the Kd values by fluorescence. See also Supplementary Fig. 2. (g) A ribbon diagram of the p300-ZZ domain (light blue) in complex with histone H3 tail (residues 1–6) (orange). (h) Electrostatic surface potential of p300-ZZ is colored blue (positive charge) and red (negative charge) with the bound histone H3 tail shown in stick.