Supplementary Figure 6: Comparative analysis of H2A.Z–H2B recognition modes for H2A.Z or H2A chaperones.

Structures in comparison are H2A.Z chaperone YL1-Z, Anp32e-ZID (4CAY) (Obri, A. et al. Nature 505, 648-53, 2014), Swr1-Z (4M6B) (Hong, J. et al. Mol Cell 53, 498-505, 2014), Chz1-Z (2JSS) (Zhou, Z. et al. Nat Struct Mol Biol 15, 868-9, 2008) and H2A chaperone FACT subunit Spt16 residue 915–943(4KHO) (Hondele, M. et al. Nature 499, 111-4, 2013) and residue 958–999 (4WNN) (Kemble, D.J. et al. Mol Cell 60, 294-306, 2015). The chaperone structures are shown in ribbon mode and histone structures in surface mode. (a), Interaction between H2A.Z-H2B dimer and H2A.Z chaperone YL1-Z (left), Anp32e-ZID (middle) and Swr1-Z (right). Structures of YL1-Z, Anp32e-ZID and Swr1-Z are colored in magenta, cyan and blue. The H2A.Z αC-cleft and H2B pocket recognized by H2A.Z chaperones are highlighted in a dotted rectangle and circle, respectively. (b), Close view of H2A.Z αC-cleft (right) and H2B pocket (left) in contact with H2A.Z chaperones. Structures of YL1-Z, Anp32e-ZID, Swr1-Z are superimposed. While YL1-Z interacts with the H2A.Z αC-cleft using the end of the α1-helix followed by a β-bend, Anp32e-ZID and Swr1-Z both use a short helix for interaction. Importantly, YL1-Z, Anp32e-ZID and Swr1-Z each bury a similar aromatic residue (Y44, F623, Y235, respectively) in the H2B pocket. (c), Structure of yeast FACT subunit Spt16 residues 915–956 (colored in green) interacting with H2A–H2B (left) and close view of the contact with H2B pocket (right). The side chain of F939 is colored in orange for clear view. (d), Structure of yeast FACT subunit Spt16 residues 958–999 (colored in orange) interacting with H2A–H2B (left) and close view of the contact with H2B pocket (right). (e), Structure comparison of YL1-Z and Chz1. Chz1 residues 63–124 (green) are shown in ribbon representation. Binding of YL1-Z and Chz1 at the H2A.Z α1–α2 patch, highlighted in the dotted circle, are mutually exclusive.