Supplementary Figure 1: Single-chain histone dimers form stable 1:1 complexes with YL1-Z (Swc2-Z).
From: Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1
(a), The single chain H2A.Z–H2B and single chain H2A–H2B used in this study. Shown on top are the sequence alignments of human and yeast single chain H2A.Z–H2B (scZB) and corresponding secondary structures. H2B (red), H2A.Z (yellow), and extended H2A.Z αC-helix (orange). Yeast-specific residues colored in red. (b), Sedimentation velocity experiments show that human YL1-Z (hYL1-Z) and Drosophila YL1-Z (dYL1-Z) mainly form a 1:1 complex with human scZB (hscZB), in both 0.2 M NaCl and 0.5 M NaCl. The svedbergs value (S) and molecular weight (kD) are shown in each figure. (c), Sedimentation equilibrium experiments show that both human YL1-Z residues 1–77 and human YL1-Z residues 12–77 form a 1:1 complex with yeast scZB in 0.1 M NaCl. Removal of 11 residues within hYL1-Z Rn-region shows no effect on stoichiometry of the complex.
