Fig. 1: Taf14_ET binds a short motif of Sth1.

a Domain organization of the ScSth1 and ScTaf14 proteins. HSA Helicase-SANT-Association domain, ATPase ATPase domain, SnAc Snf2 ATP coupling domain, EBM ET-Binding Motif, Bromo Bromodomain, YEATS Yaf9-ENL-AF9-Taf14-Sas5 shared domain, ET Extra-Terminal domain. b GST pull-down assays showed the interaction between GST-Taf14_174–244 and four different Sth1 fragments. GST-Taf14_174–244 could pull-down Sth1_1183–1359, Sth1_1183–1240, and Sth1_1199–1225, but not Sth1_1248–1359. c The interaction between Taf14_ET (Taf14_174–244) and Sth1_EBM (Sth1_1183–1240) was not affected by altering solution ionic strength, as shown by ITC measurements at three different salt concentrations. The upper panel shows the heat change upon titration; the lower panel shows the binding isotherm profile fit based on a “one binding site” model. The dissociation constant (K_D), enthalpy change (ΔH), and their fitting errors were shown. d [¹⁵N-¹H] HSQC of Taf14_174–244 at different concentrations indicated the concentration-dependent aggregation in solution. 0.05 mM, 512 scans; 0.1 mM, 128 scans; 0.2 mM, 128 scans; 0.5 mM, 32 scans. e [¹⁵N-¹H] HSQC of Taf14_174–244 at 0.5 mM concentration in the presence of 0.75 mM unlabeled Sth1_1183–1240 indicated a well-folded structure. f Circular dichroism spectra of Taf14_174–244 (0.1 mg/mL), Sth1_1183–1240 (0.1 mg/mL), Taf14_174–244-Sth1_1183–1240 (0.15 mg/mL) in 2 mM HEPES, pH 7.0, 100 mM NaF buffer.