Evidence map›Paper›PMID 37081318›Full record

ArticleNature structural & molecular biology2023

Structure of a SIN3-HDAC complex from budding yeast.

Zhouyan Guo, Chen Chu, Yichen Lu, Xiaofeng Zhang, Yihang Xiao, Mingxuan Wu, Shuaixin Gao, Catherine C L Wong, Xiechao Zhan, Chengcheng Wang

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 18 citations in OpenAlex.

  1. Alterations to the yeast chromatin landscape during hypoxia.bioRxiv : the preprint server for biology · 2026
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  12. Review
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  14. HDAC1: An Essential and Conserved Member of the Diverse ZnInternational journal of molecular sciences · 2023
    Article
  15. Histone deacetylation and cytosine methylation compartmentalize heterochromatic regions in the genome organization ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Zhouyan Guo *College of Life Sciences, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0000-0002-7232-6152
Chen Chu *College of Life Sciences, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0000-0001-5381-6909
Yichen LuKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China.
Xiaofeng ZhangKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China.ORCID http://orcid.org/0000-0002-9658-5917
Yihang XiaoDepartment of Chemistry, School of Science, Westlake University, Hangzhou, China.
Mingxuan WuDepartment of Chemistry, School of Science, Westlake University, Hangzhou, China.
Shuaixin GaoHuman Nutrition Program & James Comprehensive Cancer Center, Ohio State University, Columbus, OH, USA.
Catherine C L WongClinical Research Institute, State Key Laboratory of Complex Severe and Rare Diseases, Peking Union Medical College Hospital, Chinese Academy of Medical Science & Peking Union Medical College, Beijing, China.ORCID http://orcid.org/0000-0002-6855-2798
Xiechao ZhanKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China. zhanxiechao@westlake.edu.cn.ORCID http://orcid.org/0000-0003-3084-5656
Chengcheng WangKey Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, China. wangchengcheng@westlake.edu.cn.ORCID http://orcid.org/0000-0002-1467-9267
Westlake University · CNChinese Academy of Medical Sciences & Peking Union Medical College · CNThe Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 Å. 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.

Indexed as

Saccharomyces cerevisiae ProteinsSaccharomycetalesChromatinHistone DeacetylasesRepressor ProteinsTranscription FactorsChromatinHistone DeacetylasesRepressor ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID37081318
OpenAlexW4366506705

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.