Fig. 5: Sas3 also contains EBM, which is recognized by Taf14ET.
From: Molecular insight into interactions between the Taf14, Yng1 and Sas3 subunits of the NuA3 complex
a Domain architecture of Yng1, Taf14 and Sas3. Sequence alignment of Yng1EBM and Sas3EBM is shown on the right. b Binding curves used to determine Kd for the interaction of Taf14FL with Sas3EBM by tryptophan fluorescence. The Kd value represents average of three independent measurements, with error calculated as SD between the runs. c Superimposed 1H,15N HSQC spectra of Taf14ET recorded in the presence of increasing amounts of Sas3EBM peptide. The spectra are color coded according to the protein:peptide molar ratio. d Binding curves used to determine Kd for the interaction of Taf14ET with Sas3EBM by tryptophan fluorescence. The Kd value represents average of three independent measurements, with error calculated as SD between the runs. e–h NMR assays to monitor interactions of Taf14ET with the indicated mutants of Sas3EBM. Overlayed 1H,15N HSQC spectra of Taf14ET recorded in the presence of increasing amounts of the mutated Sas3EBM peptides are shown in (e, g, h). The spectra are color coded according to the protein:peptide molar ratio. Binding curves used to determine Kd by NMR are shown in (f). The Kd value represents average of CSPs observed in three amides ± SD. The apparent Kd values in (b, d and f) were calculated using a 1:1 stoichiometry. Source data are provided as a Source Data file.
