Fig. 3
From: Caf1 regulates the histone methyltransferase activity of Ash1 by sensing unmodified histone H3
The binding mode of CBM on Caf1. A An AlphaFold predicted structural model of Caf1 (grey) bound to CBM (1582–1616 a.a., cyan). The CBM binds to Caf1 histone H4 binding pocket, forming a clip-like structure. B Detailed interactions between Caf1 and CBM. R1604 of CBM makes extensive electrostatic interaction with carboxyl groups in the loop (366–371 a.a.) and D362/D365 residues in Caf1 (left panel). In addition, E1591 in CBM makes a salt bridge with K30 in Caf1, further stabilizing the Caf1_CBM interaction. C GST pulldown assay using GST-CBM wild-type and mutants for Caf1 binding. GST-CBMs are marked with green dots, and CBM bound Caf1 in red dots