한빛사 논문
Jung-Hoon Lee1,2,*, Daniel Bollschweiler1, Tillman Schäfer1 and Robert Huber1,2,3,4,*
1Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.
2Proteros biostructures GmbH, Bunsenstr 7a, 82152 Martinsried, Germany.
3Zentrum für Medizinische Biotechnologie, Universität Duisburg-Essen, 45117 Essen, Germany.
4Fakultät für Chemie, Technische Universität München, 85747 Garching, Germany.
*Corresponding author.
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 Hda12-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.
논문정보
관련 링크
연구자 ID
관련분야 연구자보기
소속기관 논문보기
관련분야 논문보기
해당논문 저자보기