Fig. 3: Role of hydrophobic contacts.
From: Molecular insight into interactions between the Taf14, Yng1 and Sas3 subunits of the NuA3 complex
a Electrostatic surface potential of the Taf14ET-Yng1EBM complex, with blue and red colors representing positive and negative charges, respectively. Dimeric Yng1EBM is shown as yellow and red β strands. (b-f) NMR assays to monitor interactions of Taf14ET with the indicated mutants of Yng1EBM. Overlayed 1H,15N HSQC spectra of Taf14ET recorded in the presence of increasing amounts of the mutated Yng1EBM peptides are shown in (b, c, and e). The spectra are color coded according to the protein:peptide molar ratio. Binding curves used to determine Kds by NMR are shown in (d, f). The Kd value represents average of CSPs observed in three amides ± SD. g Binding affinities of Taf14 proteins to the indicated ligands measured by aMST, bfluorescence, and cNMR. nb, no binding (h) Domain architecture of Yng1, a subunit of the NuA3 complex, and of Yng2, a subunit of the NuA4 complex. EBM sequence in Yng1 and the corresponding sequence in Yng2 are shown. The apparent Kd values in (d, f, and g) were calculated using a 1:1 stoichiometry. Source data are provided as a Source Data file.
