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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/SDS3_YEAST SDS3_YEAST] Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SDS3 is required for the HDAC activity of the complex and for the RPD3-SIN3 association.<ref>PMID:10655212</ref> <ref>PMID:11024051</ref> <ref>PMID:11405640</ref> <ref>PMID:8978024</ref>  
[https://www.uniprot.org/uniprot/SDS3_YEAST SDS3_YEAST] Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SDS3 is required for the HDAC activity of the complex and for the RPD3-SIN3 association.<ref>PMID:10655212</ref> <ref>PMID:11024051</ref> <ref>PMID:11405640</ref> <ref>PMID:8978024</ref>  
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== Publication Abstract from PubMed ==
The Rpd3L histone deacetylase (HDAC) complex is an ancient 12-subunit complex conserved in a broad range of eukaryotes that performs localized deacetylation at or near sites of recruitment by DNA-bound factors. Here we describe the cryo-EM structure of this prototypical HDAC complex that is characterized by as many as seven subunits performing scaffolding roles for the tight integration of the only catalytic subunit, Rpd3. The principal scaffolding protein, Sin3, along with Rpd3 and the histone chaperone, Ume1, are present in two copies, with each copy organized into separate lobes of an asymmetric dimeric molecular assembly. The active site of one Rpd3 is completely occluded by a leucine side chain of Rxt2, while the tips of the two lobes and the more peripherally associated subunits exhibit varying levels of flexibility and positional disorder. The structure reveals unexpected structural homology/analogy between unrelated subunits in the fungal and mammalian complexes and provides a foundation for deeper interrogations of structure, biology, and mechanism of these complexes, as well as for the discovery of HDAC complex-specific inhibitors.
Cryo-EM structure of the Saccharomyces cerevisiae Rpd3L histone deacetylase complex.,Patel AB, Qing J, Tam KH, Zaman S, Luiso M, Radhakrishnan I, He Y Nat Commun. 2023 May 27;14(1):3061. doi: 10.1038/s41467-023-38687-z. PMID:37244892<ref>PMID:37244892</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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Latest revision as of 06:48, 19 June 2024

Structure of the yeast (HDAC) Rpd3L complex

8ga8, resolution 3.50Å

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