Fig. 5: YEATS domains from Taf14 and Sas5 are Kbz readers.

a ITC analyses show that Taf14_YEATS has different binding affinities with Kbz peptides. b ITC analyses show that Sas5_YEATS could bind Kbz peptides with different binding affinities. c ITC analyses show that Yaf9_YEATS does not bind any Kbz peptides tested or that the binding affinity is beyond the detection limit. d Superimposition of Taf14_YEATS-H3K9bz and Sas5_YEATS-H3K27bz structures. The Taf14_YEATS and Sas5_YEATS are shown in yellow and green; H3K9bz and H3K27bz peptides are shown in blue and magenta. e The benzoyl groups in H3K9bz and H3K27bz peptides are inserted into a conserved binding pocket sharing nearly identical interacting networks. The residues involved in hydrophobic contacts and hydrogen bonds (orange dashed lines) are localized in two arms, embracing the benzoyl group. The red dot is the water molecule. f ITC results show the effects of Sas5_YEATS mutations on the interaction between Sas5_YEATS and H3K27bz peptide. g ITC results show the effects of Taf14_YEATS mutations on the interaction between Taf14_YEATS and H3K9bz peptide. h Superimposition of four YEATS-Kbz complex structures, including AF9-H3K9bz (gray-red), YEATS2-H3K27bz (orange-navy blue), Taf14-H3K9bz (yellow-cyan), and Sas5-H3K27bz (green-magenta). The residues at the tip regions of the benzoyl-binding pocket are different and indicated by arrows. i The acyl-binding pocket of Taf14_YEATS. Four Taf14_YEATS structures are superimposed, including Taf14-H3K9bz, Taf14-H3K9ac (PDB: 5D7E), Taf14-H3K9cr (PDB: 5IOK), and Taf14-H3K9bu (PDB: 6MIQ). The benzoyl, acetyl, crotonyl, and butyryl groups are shown in cyan, magenta, orange, and green, respectively. The tip residues of V29 and A63 are involved in the fine-tuning of pocket shapes to accommodate different acylation marks. j ITC results reveal that the mutations of tip residues on Taf14_YEAST and Sas5_YEATS have negligible effects on binding with acetylated peptides.