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-Structure paper
Title | Structural basis for the regulation of nucleosome recognition and HDAC activity by histone deacetylase assemblies. |
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Journal, issue, pages | Sci Adv, Vol. 7, Issue 2, Year 2021 |
Publish date | Jan 8, 2021 |
Authors | Jung-Hoon Lee / Daniel Bollschweiler / Tillman Schäfer / Robert Huber / |
PubMed 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 ...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-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. |
External links | Sci Adv / PubMed:33523989 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.11 - 10.6 Å |
Structure data | EMDB-11092, PDB-6z6f: EMDB-11094, PDB-6z6h: EMDB-11101, PDB-6z6o: EMDB-11102, PDB-6z6p: EMDB-11712: EMDB-11797: |
Chemicals | ChemComp-ZN: |
Source |
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Keywords | GENE REGULATION / Protein complex |