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dc.contributor.authorDanilenko, Nataliya
dc.contributor.authorLercher, Lukas
dc.contributor.authorKirkpatrick, John
dc.contributor.authorGabel, Frank
dc.contributor.authorCodutti, Luca
dc.contributor.authorCarlomagno, Teresa
dc.date.accessioned2019-09-16T12:53:14Z
dc.date.available2019-09-16T12:53:14Z
dc.date.issued2019-08-06
dc.identifier.issn2041-1723
dc.identifier.doi10.1038/s41467-019-11410-7
dc.identifier.urihttp://hdl.handle.net/10033/621940
dc.description.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 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.en_US
dc.language.isoenen_US
dc.publisherSpringer Science and Business Media LLCen_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectGeneral Biochemistry, Genetics and Molecular Biologyen_US
dc.subjectGeneral Physics and Astronomyen_US
dc.subjectGeneral Chemistryen_US
dc.titleHistone chaperone exploits intrinsic disorder to switch acetylation specificityen_US
dc.typeArticleen_US
dc.contributor.departmentHIPS, Helmholtz-Institut für Pharmazeutische Forschung Saarland, Universitätscampus E8.1 66123 Saarbrücken, Germanyen_US
dc.identifier.journalNature Communicationsen_US
dc.source.volume10
dc.source.issue1
refterms.dateFOA2019-09-16T12:53:14Z


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