Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections)

Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T, Nat Commun 10(1):3435 (2019) URL

SASDFM7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, acetylatransferase Rtt109, 2H histone chaperone Vps75 (1-225aa) in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)
Histone acetyltransferase RTT109
Histone chaperone ASF1
Histone H4
Histone H3 full-length
MWexperimental 149 kDa
MWexpected 149 kDa
log I(s) 1.46×10-1 1.46×10-2 1.46×10-3 1.46×10-4
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length small angle scattering data  s, nm-1
ln I(s)
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Guinier plot ln 1.47×10-1 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Kratky plot 1.104 0 √3 sRg
p(r)
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length pair distance distribution function Rg: 2.8 nm 0 Dmax: 9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length GROMACS model
SANS data from solutions the Asf1-H3:H4-Rtt109-Vps75 protein complex (1H Asf1-H3:H4-Rtt109, bound to 2H-labelled Vps75(1-225)) in 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pD 6.5 were collected on the D22 instrument at the ILL (Grenoble, France) using a 3He multidetector 128 linear sensitive Reuter-Stokes detector detector at a sample-detector/Collimation distance of 4 m/4 m and at a wavelength of λ = 0.6 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.9 mg/ml was measured at 25°C for 1 h.

Storage temperature = UNKNOWN

Vacuolar protein sorting-associated protein 75 (1-225 aa) (Vps75 1-225)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Dimer
Mon. MW   26.6 kDa
 
UniProt   P53853 (1-225)
Sequence   FASTA
 
Histone acetyltransferase RTT109 (Rtt109)
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Monomer
Mon. MW   50.1 kDa
 
UniProt   Q07794 (1-436)
Sequence   FASTA
 
Histone chaperone ASF1 (Asf1)
Mol. type   Protein
Olig. state   Monomer
Mon. MW   19.1 kDa
 
UniProt   P32447 (1-169)
Sequence   FASTA
 
Histone H4 (H4)
Mol. type   Protein
Organism   Xenopus laevis
Olig. state   Monomer
Mon. MW   11.4 kDa
 
UniProt   P62799 (1-103)
Sequence   FASTA
 
Histone H3 full-length (H3 FL)
Mol. type   Protein
Organism   Xenopus laevis
Olig. state   Monomer
Mon. MW   15.3 kDa
 
UniProt   Q6PI79 (1-136)
Sequence   FASTA
 
PDB ID   3Q66
 
PDB ID   3Q66