Evidence map›Paper›PMID 33512761›Full record

ArticleEMBO reports2021

Succinylation of H3K122 destabilizes nucleosomes and enhances transcription.

Lara Zorro Shahidian, Mariska Haas, Stephanie Le Gras, Sandra Nitsch, André Mourão, Arie Geerlof, Raphael Margueron, Jens Michaelis, Sylvain Daujat, Robert Schneider

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

58 citing papers in PubMed, 80 citations in OpenAlex.

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  6. Stage-Specific H3K14 and H3K23 Succinylation Orchestrates Insect Metamorphosis and Oogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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.

Lara Zorro ShahidianInstitute of Functional Epigenetics, Helmholtz Zentrum München, Neuherberg, Germany.ORCID 0000-0002-3182-9642
Mariska HaasInstitute of Biophysics, Ulm University, Ulm, Germany.
Stephanie Le GrasIGBMC, CNRS UMR7104, Inserm U1258, Université de Strasbourg, Illkirch, France.
Sandra NitschInstitute of Functional Epigenetics, Helmholtz Zentrum München, Neuherberg, Germany.
André MourãoProtein Expression and Purification Facility, Helmholtz Zentrum München, Neuherberg, Germany.
Arie GeerlofProtein Expression and Purification Facility, Helmholtz Zentrum München, Neuherberg, Germany.
Raphael MargueronInstitut Curie, INSERM U934, CNRS UMR3215, Paris, France.ORCID 0000-0002-9093-7977
Jens MichaelisInstitute of Biophysics, Ulm University, Ulm, Germany.
Sylvain DaujatIGBMC, CNRS UMR7104, Inserm U1258, Université de Strasbourg, Illkirch, France.
Robert SchneiderInstitute of Functional Epigenetics, Helmholtz Zentrum München, Neuherberg, Germany.
Helmholtz Zentrum München · DECentre National de la Recherche Scientifique · FRUniversität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone post-translational modifications (PTMs) are key players in chromatin regulation. The identification of novel histone acylations raises important questions regarding their role in transcription. In this study, we characterize the role of an acylation on the lateral surface of the histone octamer, H3K122 succinylation (H3K122succ), in chromatin function and transcription. Using chromatin succinylated at H3K122 in in vitro transcription assays, we show that the presence of H3K122succ is sufficient to stimulate transcription. In line with this, we found in our ChIP assays H3K122succ enriched on promoters of active genes and H3K122succ enrichment scaling with gene expression levels. Furthermore, we show that the co-activators p300/CBP can succinylate H3K122 and identify sirtuin 5 (SIRT5) as a new desuccinylase. By applying single molecule FRET assays, we demonstrate a direct effect of H3K122succ on nucleosome stability, indicating an important role for histone succinylation in modulating chromatin dynamics. Together, these data provide the first insights into the mechanisms underlying transcriptional regulation by H3K122succ.

Indexed as

HistonesNucleosomesChromatinGene Expression RegulationProtein Processing, Post-TranslationalChromatinHistonesNucleosomesacylationhistonessuccinylation

Identifiers

PMID33512761
PMCPMC7926236
OpenAlexW3123068255

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.