Evidence map›Paper›PMID 32766790›Full record

ArticleNucleic acids research2020

Semisynthesis of site-specifically succinylated histone reveals that succinylation regulates nucleosome unwrapping rate and DNA accessibility.

Yihang Jing, Dongbo Ding, Gaofei Tian, Ka Chun Jonathan Kwan, Zheng Liu, Toyotaka Ishibashi, Xiang David Li

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 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

47 citing papers in PubMed, 61 citations in OpenAlex.

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  18. Basic Epigenetic Mechanisms.Sub-cellular biochemistry · 2025
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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

7 authors at 2 institutions in 1 country.

Yihang JingDepartment of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Dongbo DingDivision of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
Gaofei TianDepartment of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Ka Chun Jonathan KwanDepartment of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Zheng LiuDepartment of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Toyotaka IshibashiDivision of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
Xiang David LiDepartment of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
University of Hong Kong · HKHong Kong University of Science and Technology · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Posttranslational modifications (PTMs) of histones represent a crucial regulatory mechanism of nucleosome and chromatin dynamics in various of DNA-based cellular processes, such as replication, transcription and DNA damage repair. Lysine succinylation (Ksucc) is a newly identified histone PTM, but its regulation and function in chromatin remain poorly understood. Here, we utilized an expressed protein ligation (EPL) strategy to synthesize histone H4 with site-specific succinylation at K77 residue (H4K77succ), an evolutionarily conserved succinylation site at the nucleosomal DNA-histone interface. We then assembled mononucleosomes with the semisynthetic H4K77succ in vitro. We demonstrated that this succinylation impacts nucleosome dynamics and promotes DNA unwrapping from the histone surface, which allows proteins such as transcription factors to rapidly access buried regions of the nucleosomal DNA. In budding yeast, a lysine-to-glutamic acid mutation, which mimics Ksucc, at the H4K77 site reduced nucleosome stability and led to defects in DNA damage repair and telomere silencing in vivo. Our findings revealed this uncharacterized histone modification has important roles in nucleosome and chromatin dynamics.

Indexed as

Bacterial ProteinsChromatinDNAFluorescence Resonance Energy TransferHistonesLexA Repressor ProteinLysineNucleosomesProtein Processing, Post-TranslationalRecombinant ProteinsSaccharomyces cerevisiaeSerine EndopeptidasesXenopus ProteinsBacterial ProteinsChromatinDNAHistonesLexA Repressor ProteinLysineNucleosomesRecombinant ProteinsSerine EndopeptidasesXenopus Proteins

Identifiers

PMID32766790
PMCPMC7515725
OpenAlexW3048260234

What OpenQuestion holds

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LicenceCC BY
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.