8hpo
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/UME1_YEAST UME1_YEAST] Catalytic component of the RPD3 histone deacetylase complexes RPD3C(L) and RPD3C(S) 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.<ref>PMID:12954623</ref> <ref>PMID:16286008</ref> <ref>PMID:9234739</ref> | [https://www.uniprot.org/uniprot/UME1_YEAST UME1_YEAST] Catalytic component of the RPD3 histone deacetylase complexes RPD3C(L) and RPD3C(S) 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.<ref>PMID:12954623</ref> <ref>PMID:16286008</ref> <ref>PMID:9234739</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | SIN3-HDAC (histone deacetylases) complexes have important roles in facilitating local histone deacetylation to regulate chromatin accessibility and gene expression. Here, we present the cryo-EM structure of the budding yeast SIN3-HDAC complex Rpd3L at an average resolution of 2.6 A. The structure reveals that two distinct arms (ARM1 and ARM2) hang on a T-shaped scaffold formed by two coiled-coil domains. In each arm, Sin3 interacts with different subunits to create a different environment for the histone deacetylase Rpd3. ARM1 is in the inhibited state with the active site of Rpd3 blocked, whereas ARM2 is in an open conformation with the active site of Rpd3 exposed to the exterior space. The observed asymmetric architecture of Rpd3L is different from those of available structures of other class I HDAC complexes. Our study reveals the organization mechanism of the SIN3-HDAC complex and provides insights into the interaction pattern by which it targets histone deacetylase to chromatin. | ||
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| - | Structure of a SIN3-HDAC complex from budding yeast.,Guo Z, Chu C, Lu Y, Zhang X, Xiao Y, Wu M, Gao S, Wong CCL, Zhan X, Wang C Nat Struct Mol Biol. 2023 Apr 20. doi: 10.1038/s41594-023-00975-z. PMID:37081318<ref>PMID:37081318</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 8hpo" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Cryo-EM structure of a SIN3/HDAC complex from budding yeast
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