Histone chaperone exploits intrinsic disorder to switch acetylation specificity

Histone chaperone exploits intrinsic disorder to switch acetylation specificity

Histone chaperones have been shown to control the activity and specificity of histone-modifying enzymes. Here the authors establish a structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4, finding that Vps75 promotes K9-acetylation by engaging th...

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Bibliographic Details
Main Authors: Nataliya Danilenko, Lukas Lercher, John Kirkpatrick, Frank Gabel, Luca Codutti, Teresa Carlomagno
Format: Article
Language:English
Published: Nature Publishing Group 2019-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-11410-7
Description
Summary:Histone chaperones have been shown to control the activity and specificity of histone-modifying enzymes. Here the authors establish a structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4, finding that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain.
ISSN:2041-1723

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