Histone chaperone exploits intrinsic disorder to switch acetylation specificity.

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

SASDFL3 – All 1H histone acetyltransferase Rtt109 complex with histones H3 and H4 and histone chaperones Asf1 and Vps75 (acquired in 100% v/v D2O)

Vacuolar protein sorting-associated protein 75 (1-225 aa)
Histone acetyltransferase RTT109
Histone chaperone ASF1
Histone H3.2 (35-135 aa)
Histone H4
MWexperimental 145 kDa
MWexpected 145 kDa
log I(s) 3.10×10-1 3.10×10-2 3.10×10-3 3.10×10-4
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H3.2 (35-135 aa) Histone H4 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 H3.2 (35-135 aa) Histone H4 Guinier plot ln 3.10×10-1 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Vacuolar protein sorting-associated protein 75 (1-225 aa) Histone acetyltransferase RTT109 Histone chaperone ASF1 Histone H3.2 (35-135 aa) Histone H4 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 H3.2 (35-135 aa) Histone H4 pair distance distribution function Rg: 3.5 nm 0 Dmax: 11.8 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 H3.2 (35-135 aa) Histone H4 HADDOCK model

SANS data from solutions of the all 1H Asf1-H3:H4-Rtt109-Vps75 protein complex in 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pD 6.5 were collected on the KWS1 instrument at FRM2 (Munich, Germany) using a SANS 6Li-Scintillator 1 mm thickness + photomultiplier detector. Data were collected at two sample detector positions: 1) 1.5 m for 1 hr using a neutron wavelength of 0.5 nm and; 2) 4 m for 2 hrs using a neutron wavelength of 0.5 nm. Both data sets were recorded on the same sample at 2.35 mg/mL, measured at 25°C.

Vacuolar protein sorting-associated protein 75 (1-225 aa) (Vps75 1-225)
Mol. type   Protein
Organism   Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Olig. state   Dimer
Mon. MW   26.6 kDa
 
UniProt   P53853 (1-225)
Sequence   FASTA
 
Histone acetyltransferase RTT109 (Rtt109)
Mol. type   Protein
Organism   Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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 H3.2 (35-135 aa) (H3 (35-135))
Mol. type   Protein
Organism   Xenopus laevis
Olig. state   Monomer
Mon. MW   11.7 kDa
 
UniProt   P84233 (35-135)
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
 
PDB code   6O22