Extended Data Fig. 5: The bromodomains of Gcn5 and Spt7 contribute to SAGA dimerization.
a, Amino acid sequences of the S. cerevisiae histone H3-K14ac and Ada3-K8ac, K14ac and K182ac. H3 lysine 14 and Ada3 lysine 8, 14 and 182 are highlighted in red. b, The molecular docking of Gcn5 bromodomain with Ada3 peptide acetylated at K182 (Ada3-EK182acR). c, The molecular docking of Spt7 bromodomain with Ada3 peptide acetylated at K8 (Ada3-GK8acL). d, The molecular docking of Spt7 bromodomain with Ada3 peptide acetylated at K14 (Ada3-EK14acL). e, Coomassie Blue staining of recombinantly purified Gcn5 bromodomain and Spt7 bromodomain. f, Isothermal titration calorimetry (ITC) assays were performed with purified recombinant Gcn5 bromodomain, Spt7 bromodomain and unacetylated Ada3 peptides. g, Silver staining of purified Wt SAGA, SAGA Gcn5 Bro-mut and Spt7 Bro-mut. h, Gcn5 bromodomain and Spt7 bromodomain are required for SAGA self-association as determined by in vivo Co-IP. i, Glycerol density gradient centrifugation analysis of Wt SAGA or SAGA Gcn5/Spt7 Bro-mut purified from cells grown in 2% sucrose-containing media. j, Quantification of fractions in Extended Data Fig. 5i. For Extended Data Fig. 5f, the quantitative data represent means ± SE (n=3). For Extended Data Fig. 5e, g, h, i, shown is the typical example of two biological independent experiments.
