Fig. 1: Yng1 contains EBM, which is recognized by Taf14ET.
From: Molecular insight into interactions between the Taf14, Yng1 and Sas3 subunits of the NuA3 complex
a Schematic of the yeast histone acetyltransferase NuA3 complex, which catalyzes acetylation of lysine 14 in histone H3 (H3K14ac). b Domain architecture of Taf14 and Yng1. H3K4me3, H3K9acyl and DNA, the known ligands for the PHD finger of Yng1, the YEATS domain of Taf14, and the linker of Taf14, respectively, are indicated. c Overlayed 1H,15N HSQC spectra of Taf14FL recorded in the presence of increasing amounts of Yng1EBM peptide. The spectra are color coded according to the protein:peptide molar ratio. d MST binding curve for the interaction of Taf14FL with Yng1EBM. The Kd  value represents average of three independent measurements ± SEM, and error bars represent SEM for each point. n = 3. e Tryptophan fluorescence binding curves for the interaction of Taf14FL with Yng1EBM. The Kd value represents average of three independent measurements, with error calculated as SD between the runs. f Superimposed 1H,15N HSQC spectra of Taf14ET recorded in the presence of increasing amount of Yng1EBM. The spectra are color coded according to the protein:peptide molar ratio. g Tryptophan fluorescence binding curves for the interaction of Taf14ET with Yng1EBM. The Kd value represents average of three independent measurements, with error calculated as SD between the runs. h, i Superimposed 1H,15N HSQC spectra of Taf14ET (h) or Taf14YEATS (i) recorded in the presence of increasing amounts of Yng1EBM-PHD (h) or Yng1EBM peptide (i). The spectra are color coded according to the protein:ligand molar ratio. The apparent Kd values in (d, e and g) were calculated using a 1:1 stoichiometry. Source data are provided as a Source Data file.
