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TitleHistone chaperone exploits intrinsic disorder to switch acetylation specificity.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 3435, Year 2019
Publish dateAug 6, 2019
AuthorsNataliya Danilenko / Lukas Lercher / John Kirkpatrick / Frank Gabel / Luca Codutti / Teresa Carlomagno /
PubMed AbstractHistones, the principal protein components of chromatin, contain long disordered sequences, which are extensively post-translationally modified. Although histone chaperones are known to control both ...Histones, the principal protein components of chromatin, contain long disordered sequences, which are extensively post-translationally modified. Although histone chaperones are known to control both the activity and specificity of histone-modifying enzymes, the mechanisms promoting modification of highly disordered substrates, such as lysine-acetylation within the N-terminal tail of histone H3, are not understood. Here, to understand how histone chaperones Asf1 and Vps75 together promote H3 K9-acetylation, we establish the solution structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4. We show that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain, thereby confining the H3 tail to a wide central cavity faced by the Rtt109 active site. These fuzzy interactions between disordered domains achieve localization of lysine residues in the H3 tail to the catalytic site with minimal loss of entropy, and may represent a common mechanism of enzymatic reactions involving highly disordered substrates.
External linksNat Commun / PubMed:31387991 / PubMed Central
MethodsSAS (neutron source) / NMR (solution) / small angle scattering
Structure data

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

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
Method: SAXS/SANS

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
Method: SAXS/SANS

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
Method: SAXS/SANS

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
Method: SAXS/SANS

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
Method: SAXS/SANS

PDB-6o22:
Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate.
Method: SOLUTION NMR / SOLUTION SCATTERING

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • xenopus laevis (African clawed frog)
KeywordsCHAPERONE

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