Fig. 5
From: Histone chaperone exploits intrinsic disorder to switch acetylation specificity
The disordered Vps75 CTAD guides substrate specificity. a The SANS-derived ab initio envelopes of Asf1–H3:H4–Rtt109–Vps7521–225 (middle) and Asf1–H335–135:H4–Rtt109–Vps7521–225 (right) display a central empty cavity, which is filled by scattering units in the complex containing full-length proteins (left). Therefore the H3 tail does not enter the cavity in the absence of the Vps75 CTAD. b Overlay of 1H-15N spectra of Vps752 in isolation and as part of either Asf1–H3:H4–Rtt109–Vps752 or Asf1–H329–135:H4–Rtt109–Vps752. Only signals of the Vps75 CTAD are visible. In Asf1–H3:H4–Rtt109–Vps752, the CTADs of Vps75(A) and Vps75(B) display different chemical shifts: the peaks of one of the two CTADs remain in the same positions as those from Vps752, while those of the other CTAD move to new positions. The peaks of residues 234–246 move less far in Asf1–H335–135:H4–Rtt109–Vps752 (CSP plot, bottom). c TALOS-N CS analysis of Vps75226–264 in the context of full-length Vps752 shows that the Vps75 tail is disordered. The same narrow CS dispersion is observed in the full complex (Supplementary Fig. 9). d, e Time-courses (left) of K56- (d) and K9-acetylation (e) quantified by dot-blot assays (right). The assays and data-analysis were done as described in the legend to Fig. 2. Source data are provided as a Source Data file
