Fig. 6: Comparison of structural conserved YET and BET-family proteins.

a Sequence alignments of the ET domains from representative members of the YET family (yTaf14, ySas5, hAF9, and hENL) and the BET family (yBdf1, yBdf2, hBRD3, and hBRD4). Secondary structure assignments (based on the Taf14_ET structure) are shown as cylinders (α-helices) and arrows (β-strands). The conserved hydrophobic residues critical for peptide binding are highlighted in yellow. The critical residues involved in the internal hydrophobic core formation are highlighted in gray. The YET-specific element (β_YET) and the BET-specific element (α_BET) are shown. b Structural comparison of the Taf14_ET–Sth1_EBM complex with BRD4_ET-NSD3_EBM (PDB: 2NCZ), with BRD3_ET-CHD4_EBM (PDB: 6BGG), and with AF9_ET-AF4_EBM (PDB: 2LM0). c Identification of the conserved hydrophobic interfaces common among these complex structures. The structurally equivalent residues are labeled. d GST pull-down assays revealed the differential binding interactions between Sumo-Sth1_1183–1240 and the various GST-tagged ET domains. e Representative images of the AF9_ET-GFP and BRD4_ET-GFP fusion proteins in the droplet formation buffer (25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 10% PEG8000) at the final concentration indicated. The scale bars indicate 10 µm.