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Structural basis for the regulation of nucleosome recognition and HDAC activity by histone deacetylase assemblies

MPS-Authors
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Lee,  Jung-Hoon
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Bollschweiler,  Daniel
Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Schäfer,  Tillmann
Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Huber,  Robert
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Lee, J.-H., Bollschweiler, D., Schäfer, T., & Huber, R. (2021). Structural basis for the regulation of nucleosome recognition and HDAC activity by histone deacetylase assemblies. Science Advances, 7(2): eabd4413. doi:10.1126/sciadv.abd4413.


Cite as: http://hdl.handle.net/21.11116/0000-0007-F216-F
Abstract
The chromatin-modifying histone deacetylases (HDACs) remove acetyl groups from acetyl-lysine residues in histone amino-terminal tails, thereby mediating transcriptional repression. Structural makeup and mechanisms by which multisubunit HDAC complexes recognize nucleosomes remain elusive. Our cryo-electron microscopy structures of the yeast class II HDAC ensembles show that the HDAC protomer comprises a triangle-shaped assembly of stoichiometry Hda1(2)-Hda2-Hda3, in which the active sites of the Hda1 dimer are freely accessible. We also observe a tetramer of protomers, where the nucleosome binding modules are inaccessible. Structural analysis of the nucleosome-bound complexes indicates how positioning of Hda1 adjacent to histone H2B affords HDAC catalysis. Moreover, it reveals how an intricate network of multiple contacts between a dimer of protomers and the nucleosome creates a platform for expansion of the HDAC activities. Our study provides comprehensive insight into the structural plasticity of the HDAC complex and its functional mechanism of chromatin modification.