Fig. 4: Taf14_ET recognizes a conserved motif on partner proteins.

a Sequence alignments of the Taf14-binding motifs present in the Sth1, Snf5, Ino80, Taf2, Sas3, and Tfg1 proteins. The consensus sequence is Φ × Φ + Φ + Φ, where Φ stands for hydrophobic residues, + stands for a positively charged residue, and × stands for any amino acid. The dissociation constants determined by ITC assays were shown. b [¹⁵N-¹H] HSQC of Taf14_ET (1 mM) in the presence of unlabeled Snf5_771–800, Ino80_368–390, Sas3_111–129, and Taf2_1393–1406 (1.5 mM). They all show similar chemical shift patterns that initially observed for the Taf14_ET–Sth1_EBM complex. c ITC measurements reveal that mutations in hydrophobic residues of the Snf5 binding motif weaken the Taf14_ET–Snf5_EBM interaction. M4 stands for the Snf5 L785A/L787A/I789A/L791A mutation. The dissociation constant (K_D), enthalpy change (ΔH), and their fitting errors from one ITC plot were shown. d ITC measurements reveal that mutations in hydrophobic residues of the Ino80 binding motif weaken the Taf14_ET–Ino80_EBM interaction. M4 stands for the Ino80 L371A/I373A/I375A/L377A mutation.