Evidence map›Paper›PMID 33231641›Full record

ArticleNucleic acids research2020

Histone sumoylation promotes Set3 histone-deacetylase complex-mediated transcriptional regulation.

Hong-Yeoul Ryu, Dejian Zhao, Jianhui Li, Dan Su, Mark Hochstrasser

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 52 citations in OpenAlex.

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  15. Crosstalk of ubiquitin system and non-coding RNA in fibrosis.International journal of biological sciences · 2024
    Review
  16. Article
  17. Article
  18. Review
  19. Histone modification inComputational and structural biotechnology journal · 2023
    Review
  20. Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023
    Review
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

5 authors at 2 institutions in 2 countries.

Hong-Yeoul RyuSchool of Life Sciences, BK21 Plus KNU Creative BioResearch Group, College of National Sciences, Kyungpook National University, Daegu 41566, Republic of Korea.
Dejian ZhaoYale Center for Genome Analysis, Yale University, New Haven, CT 06520, USA.
Jianhui LiDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Dan SuDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Mark HochstrasserDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Yale University · USKyungpook National University · KR

Funding

Mechanisms of Cell Regulation and Manipulation by the Ubiquitin SystemR35GM136325 · NIGMS · YALE UNIVERSITY · PI Mark W Hochstrasser · 2020 to 2026
$6.5M
NIGMS NIH HHS R35 GM136325
6 · The paper itself

Abstract

Histones are substrates of the SUMO (small ubiquitin-like modifier) conjugation pathway. Several reports suggest histone sumoylation affects transcription negatively, but paradoxically, our genome-wide analysis shows the modification concentrated at many active genes. We find that trans-tail regulation of histone-H2B ubiquitylation and H3K4 di-methylation potentiates subsequent histone sumoylation. Consistent with the known control of the Set3 histone deacetylase complex (HDAC) by H3K4 di-methylation, histone sumoylation directly recruits the Set3 complex to both protein-coding and noncoding RNA (ncRNA) genes via a SUMO-interacting motif in the HDAC Cpr1 subunit. The altered gene expression profile caused by reducing histone sumoylation matches well to the profile in cells lacking Set3. Histone H2B sumoylation and the Set3 HDAC coordinately suppress cryptic ncRNA transcription initiation internal to mRNA genes. Our results reveal an elaborate co-transcriptional histone crosstalk pathway involving the consecutive ubiquitylation, methylation, sumoylation and deacetylation of histones, which maintains transcriptional fidelity by suppressing spurious transcription.

Indexed as

Protein Processing, Post-TranslationalTranscription, GeneticAcetylationCyclophilin AGene Expression Regulation, FungalHistone DeacetylasesHistonesMethylationRNARNA, UntranslatedSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSumoylationUbiquitinUbiquitinationCPR1 protein, S cerevisiaeCyclophilin AHistone Deacetylaseshistone H3 trimethyl Lys4HistonesRNARNA, UntranslatedSaccharomyces cerevisiae ProteinsSet3 protein, S cerevisiaeUbiquitin

Identifiers

PMID33231641
PMCPMC7708062
OpenAlexW3110420933

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

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.