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 Aug 6)

URL: https://www.sasbdb.org/project/715/

Submitted to SASBDB: 2019 Jun 17 Published in SASBDB: 2019 Jul 10

SASDFK7 – Complex with 1H histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O 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, Institut Laue-Langevin (ILL) on 2016 Nov 14 RgGuinier 1.9 nm Dmax 5.5 nm

SASDFL7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, 2H acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) in 42% v/v D2O 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 H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5 Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14 RgGuinier 3.4 nm Dmax 10.5 nm

SASDFM7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, acetylatransferase Rtt109, 2H histone chaperone Vps75 (1-225aa) in 42% v/v D2O 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 H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5 Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14 RgGuinier 2.7 nm Dmax 9.0 nm

SASDFN7 – Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4, histone chaperones Asf1 and Vps75 (1-225aa) (acquired in 100% v/v D2O) 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 H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 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, Institut Laue-Langevin (ILL) on 2018 May 30 RgGuinier 3.5 nm Dmax 11.0 nm

SASDFP7 – Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4 and histone chaperones Asf1 and Vps75, all full-length, acquired in 100% v/v D2O Sample: Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5 Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9 RgGuinier 3.5 nm Dmax 11.5 nm

SASDFQ7 – Complex with 1H histone chaperone Vps75, histones H3 and H4, 2H histone chaperone Asf1, histone acetyltransferase Rtt109, acquired in 42% v/v D2O Sample: Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein Histone chaperone ASF1 monomer, 19 kDa protein Histone H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae protein Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5 Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Jun 9 RgGuinier 3.1 nm Dmax 9.5 nm