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

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.

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 Creators:
Lee, Jung-Hoon1, Author              
Bollschweiler, Daniel2, Author              
Schäfer, Tillmann2, Author              
Huber, Robert1, Author              
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1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              

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Free keywords: CRYO-EM; INSIGHTS; VISUALIZATION; ACTIVATION; MECHANISM; DOMAIN; RPD3Science & Technology - Other Topics;
 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.

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Language(s): eng - English
 Dates: 2021-01
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000606331400022
DOI: 10.1126/sciadv.abd4413
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Title: Science Advances
  Other : Sci. Adv.
Source Genre: Journal
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Publ. Info: Washington : AAAS
Pages: - Volume / Issue: 7 (2) Sequence Number: eabd4413 Start / End Page: - Identifier: ISSN: 2375-2548
CoNE: https://pure.mpg.de/cone/journals/resource/2375-2548