Evidence map›Paper›PMID 33580188›Full record

ArticleCommunications biology2021

Histone variant H2A.B-H2B dimers are spontaneously exchanged with canonical H2A-H2B in the nucleosome.

Rina Hirano, Yasuhiro Arimura, Tomoya Kujirai, Mikihiro Shibata, Aya Okuda, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Hitoshi Kurumizaka

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Epigenetic regulation and ROS signaling in plant stress adaptation: an integrated framework.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
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  16. Mitotic drive in asymmetric epigenetic inheritance.Biochemical Society transactions · 2022
    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 at 4 institutions in 2 countries.

Rina HiranoLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0001-8871-6166
Yasuhiro ArimuraLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0002-1903-6076
Tomoya KujiraiLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Mikihiro ShibataNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa, Japan.ORCID 0000-0001-5041-3979
Aya OkudaInstitute for Integrated Radiation and Nuclear Science (KURNS), Kyoto University, Sennan-gun, Osaka, Japan.ORCID 0000-0002-6222-8364
Ken MorishimaInstitute for Integrated Radiation and Nuclear Science (KURNS), Kyoto University, Sennan-gun, Osaka, Japan.ORCID 0000-0003-1091-3850
Rintaro InoueInstitute for Integrated Radiation and Nuclear Science (KURNS), Kyoto University, Sennan-gun, Osaka, Japan.
Masaaki SugiyamaInstitute for Integrated Radiation and Nuclear Science (KURNS), Kyoto University, Sennan-gun, Osaka, Japan.
Hitoshi KurumizakaLaboratory of Chromatin Structure and Function, Institute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan. kurumizaka@iqb.u-tokyo.ac.jp.ORCID 0000-0001-7412-3722
Kyoto University Research Reactor Institute · JPThe University of Tokyo · JPKanazawa University · JPQuantitative BioSciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

H2A.B is an evolutionarily distant histone H2A variant that accumulates on DNA repair sites, DNA replication sites, and actively transcribing regions in genomes. In cells, H2A.B exchanges rapidly in chromatin, but the mechanism has remained enigmatic. In the present study, we found that the H2A.B-H2B dimer incorporated within the nucleosome exchanges with the canonical H2A-H2B dimer without assistance from additional factors, such as histone chaperones and nucleosome remodelers. High-speed atomic force microscopy revealed that the H2A.B nucleosome, but not the canonical H2A nucleosome, transiently forms an intermediate "open conformation", in which two H2A.B-H2B dimers may be detached from the H3-H4 tetramer and bind to the DNA regions near the entry/exit sites. Mutational analyses revealed that the H2A.B C-terminal region is responsible for the adoption of the open conformation and the H2A.B-H2B exchange in the nucleosome. These findings provide mechanistic insights into the histone exchange of the H2A.B nucleosome.

Indexed as

Chromatin Assembly and DisassemblyBinding SitesDNAHistonesHumansMicroscopy, Atomic ForceNucleosomesProtein BindingProtein ConformationProtein MultimerizationStructure-Activity RelationshipTime FactorsDNAHistonesNucleosomes

Identifiers

PMID33580188
PMCPMC7881002
OpenAlexW3129144744

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.