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

SASDFQ7 – Complex with 1H histone chaperone Vps75, histones H3 and H4, 2H histone chaperone Asf1, histone acetyltransferase Rtt109, acquired in 42% v/v D2O

Histone acetyltransferase RTT109
Histone chaperone ASF1
Histone H4
Histone H3 full-length
Vacuolar protein sorting-associated protein 75 full-length
MWexperimental 157 kDa
MWexpected 157 kDa
log I(s) 1.69×10-1 1.69×10-2 1.69×10-3 1.69×10-4
Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Vacuolar protein sorting-associated protein 75 full-length small angle scattering data  s, nm-1
ln I(s)
Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Vacuolar protein sorting-associated protein 75 full-length Guinier plot ln 1.69×10-1 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Vacuolar protein sorting-associated protein 75 full-length Kratky plot 1.104 0 √3 sRg
p(r)
Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H4 Histone H3 full-length Vacuolar protein sorting-associated protein 75 full-length pair distance distribution function Rg: 3.1 nm 0 Dmax: 9.5 nm

Data validation

There are no models related to this curve.

SANS data from solutions the Asf1-H3:H4-Rtt109-Vps75 protein complex (1H Vps75-H3:H4, bound to 2H-labelled Rtt109-Asf1) in 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% 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 3.25 mg/ml was measured at 25°C for 2 h.

Storage temperature = UNKNOWN

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
 
Vacuolar protein sorting-associated protein 75 full-length (Vps75 (FL))
Mol. type   Protein
Organism   Saccharomyces cerevisiae
Olig. state   Dimer
Mon. MW   30.6 kDa
 
UniProt   P53853 (1-264)
Sequence   FASTA