Evidence map›Paper›PMID 39511190›Full record

ArticleNature communications2024

The BAF complex enhances transcription through interaction with H3K56ac in the histone globular domain.

Kwangbeom Hyun, Jihye Ahn, Hyoungmin Kim, Jihyun Kim, Yong-In Kim, Hee-Sung Park, Robert G Roeder, J Eugene Lee, Jaehoon Kim

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
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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

9 authors.

Kwangbeom HyunDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, South Korea.ORCID 0000-0002-2377-3642
Jihye AhnDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, South Korea.
Hyoungmin KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, South Korea.
Jihyun KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, South Korea.ORCID 0000-0002-4292-1911
Yong-In KimCenter for Bioanalysis, Korea Research Institute of Standards and Science, Daejeon, 34113, South Korea.ORCID 0000-0002-2877-5110
Hee-Sung ParkDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon, 34141, South Korea.ORCID 0000-0001-8645-0405
Robert G RoederLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY, 10065, USA.ORCID 0000-0003-3865-8572
J Eugene LeeDivision of Biomedical Metrology, Korea Research Institute of Standards and Science, Daejeon, 34113, South Korea. jinhwan.lee@kriss.re.kr.ORCID 0009-0000-9091-8795
Jaehoon KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, South Korea. kimjaehoon@kaist.edu.ORCID 0000-0003-4035-0438

Funding

National Research Foundation of Korea (NRF) NRF-2018R1A5A1024261National Research Foundation of Korea (NRF) NRF-2021R1A6A3A01087387
6 · The paper itself

Abstract

Histone post-translational modifications play pivotal roles in eukaryotic gene expression. To date, most studies have focused on modifications in unstructured histone N-terminal tail domains and their binding proteins. However, transcriptional regulation by chromatin-effector proteins that directly recognize modifications in histone globular domains has yet to be clearly demonstrated, despite the richness of their multiple modifications. Here, we show that the ATP-dependent chromatin-remodeling BAF complex stimulates p53-dependent transcription through direct interaction with H3K56ac located on the lateral surface of the histone globular domain. Mechanistically, the BAF complex recognizes nucleosomal H3K56ac via the DPF domain in the DPF2 subunit and exhibits enhanced nucleosome-remodeling activity in the presence of H3K56ac. We further demonstrate that a defect in H3K56ac-BAF complex interaction leads to impaired p53-dependent gene expression and DNA damage responses. Our study provides direct evidence that histone globular domain modifications participate in the regulation of gene expression.

Indexed as

Chromatin Assembly and DisassemblyDNA-Binding ProteinsHistonesTumor Suppressor Protein p53AcetylationDNA DamageGene Expression RegulationHEK293 CellsHumansNucleosomesProtein BindingProtein DomainsProtein Processing, Post-TranslationalTranscription FactorsTranscription, GeneticDNA-Binding ProteinsHistonesNucleosomesTranscription FactorsTumor Suppressor Protein p53

Identifiers

PMID39511190
PMCPMC11544104

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.