Fig. 2
From: Caf1 regulates the histone methyltransferase activity of Ash1 by sensing unmodified histone H3
Caf1 utilizes the H4 binding pocket to interact with Ash1_CBM. A The crystal structures of Caf1-histone H31–21 complex (blue, PDB ID: 2yba) and Caf1-H4 helix131–41 (green, PDB ID: 3c9c) is shown in one Caf1. B The histone H3 binding pocket is located at the central pore of Caf1. A1 and R2 residues of H3 N-terminal tail are coordinated with E235, D252 and E279 of Caf1. C Caf1 utilizes a pocket located at the side of the WD40 β-barrel structure for H4 binding. The first helix of histone H431–41 is accommodated with the carboxyl groups of D362 and D365, and the backbone carbonyl groups in a loop (366–371 a.a.) in Caf1. D GST pulldown assay using GST-CBM and Caf1 and Caf1 mutants. Caf1 H3 binding mut has mutations of E235Q/D252K/E279Q in Caf1, and Caf1 H4 binding mutant has mutations of D362A/D365A in Caf1