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 Aug 6)
PMID: 31387991
doi: 10.1038/s41467-019-11410-7
Submitted to SASBDB: 2019 Feb 27
Published in SASBDB:

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 RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 3
RgGuinier 3.5 nm
Dmax 11.8 nm

SASDFM3 – Complex with 1H histone chaperone Asf1 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1H Asf1-H3:H4, 2H Rtt109-Vps75) acquired in 100% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 4
RgGuinier -2.8 nm

SASDFN3 – Complex with 1H histone chaperones Asf1 and Vps75 and histones H3 and H4, 70%-2H histone acetyltransferase Rtt109 (1H Asf1-H3:H4-Vps75, 2H(70%) Rtt109) acquired in 100% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 4
RgGuinier 3.3 nm
Dmax 10.5 nm

SASDFP3 – Complex with 1H histone chaperone Asf1, acetyltransferase Rtt109 and histones H3 and H4, 70%-2H histone chaperone Vps75 (1H Asf1-H3:H4-Rtt109, 2H(70%) Vps75) acquired in 100% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at D22, ILL on 2018 May 29
RgGuinier 2.8 nm
Dmax 9.5 nm

SASDFQ3 – Complex with 1H histone acetyltransferase Rtt109 and histones H3 and H4, 2H histone chaperones Asf1 and Vps75 (1H Rtt109-H3:H4, 2H Asf1-Vps75) acquired in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 5
RgGuinier 3.5 nm
Dmax 11.0 nm

SASDFR3 – Complex with 1H histone chaperone Vps75 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Asf1 (1H Vps75-H3:H4, 2H Rtt109-Asf1) acquired in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 5
RgGuinier 3.1 nm
Dmax 10.5 nm