Supplementary Figure 1: YL1 specifically associates with the H2A.Z complex.
From: Molecular basis and specificity of H2A.Z–H2B recognition and deposition by the histone chaperone YL1
a) Silver staining of proteins associated with double immuno-affinity (FLAG-HA) purified e-H2A.com and e-H2A.Z.com complexes.
b) Western blotting analysis of the e-H2A.com and e-H2A.Z.com complexes shown in (a). Each complex was probed for the presence of the tagged protein (anti-HA) as well as for YL1, ANP32E, H2A and H2A.Z.
c) Mass spectrometry identification of additional proteins associated with e-H2A.com shown in (a). For each identified protein the number of unique peptides is given.
d) Mass spectrometry identification of additional proteins associated with e-H2A.Z.com shown in (a). For each identified protein the number of unique peptides is given.
e) Mass spectrometry identification of additional proteins associated with e-YL1.com shown in Figure 1a. For each identified protein the number of unique peptides is given.
f) Alignment of the YL1–ZID sequences from vertebrates, insects, plants and fungi. Conservation of the residues is represented by shades of blue. Numbering above and underneath the sequences corresponds to YL1 sequences from human and S. cerevisiae (yeast SWC2), respectively. Secondary structure elements of human YL1, as seen in the structure, are displayed above the alignment (helices, cylinders; coils, lines). The various regions of the YL1–ZID described in the text are indicated (ZIDN, ZIDM1, ZIDM2, ZIDC). Stars above and underneath the alignment mark residues of human YL1 and yeast SWC2 that were mutated in our study: m1 mutant (dark blue), m2 mutant (light blue), and m1m2 mutant (combination of m1 and m2 mutants).
