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8HY0

Composite cryo-EM structure of the histone deacetylase complex Rpd3S in complex with nucleosome

Summary for 8HY0
Entry DOI10.2210/pdb8hy0/pdb
EMDB information35084 35217 35218 35219 35220 35221
DescriptorHistone H3, RCO1 isoform 1, ZINC ION, ... (11 entities in total)
Functional Keywordshistone deacetylase complex, nucleosome, gene regulation
Biological sourceXenopus laevis (African clawed frog)
More
Total number of polymer chains16
Total formula weight798519.05
Authors
Cui, H.,Wang, H. (deposition date: 2023-01-05, release date: 2023-09-27, Last modification date: 2023-12-27)
Primary citationLi, W.,Cui, H.,Lu, Z.,Wang, H.
Structure of histone deacetylase complex Rpd3S bound to nucleosome.
Nat.Struct.Mol.Biol., 30:1893-1901, 2023
Cited by
PubMed Abstract: Crosstalk between histone modifications represents a fundamental epigenetic mechanism in gene regulation. During the transcription elongation process, the histone deacetylase complex Rpd3S is recruited to H3K36-methylated nucleosomes to suppress cryptic transcription initiation. However, how subunits of Rpd3S are assembled and coordinated to recognize nucleosomal substrates and exert their deacetylation function remains unclear. Here we report the structure of Saccharomyces cerevisiae Rpd3S deacetylase bound to H3K36me3-modified nucleosome at 3.1 Å resolution. It shows that Sin3 and Rco1 subunits orchestrate the assembly of the complex and mediate its contact with nucleosome at multiple sites, with the Sin3-DNA interface as a pivotal anchor. The PHD1 domain of Rco1 recognizes the unmodified H3K4 and places the following H3 tail toward the active site of Rpd3, while the chromodomain of Eaf3 subunit recognizes the H3K36me3 mark and contacts both nucleosomal and linker DNA. The second copy of Eaf3-Rco1 is involved in neighboring nucleosome binding. Our work unravels the structural basis of chromatin targeting and deacetylation by the Rpd3S complex.
PubMed: 37798513
DOI: 10.1038/s41594-023-01121-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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건을2024-11-06부터공개중

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