Evidence map›Paper›PMID 29945241›Full record

ArticleNucleic acids research2018

Histone H2A variants confer specific properties to nucleosomes and impact on chromatin accessibility.

Akihisa Osakabe, Zdravko J Lorkovic, Wataru Kobayashi, Hiroaki Tachiwana, Ramesh Yelagandula, Hitoshi Kurumizaka, Frédéric Berger

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 97 citations in OpenAlex.

  1. H2AC19 promotes lung adenocarcinoma progressionActa pharmaceutica Sinica. B · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Histone variant H2A.W7 represses meiotic crossover formation inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. DDM1 Maintains Heterochromatin by Regulating Histone Variants.International journal of molecular sciences · 2025
    Review
  8. The histone variant H2A.W restricts heterochromatic crossovers inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
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 2 countries.

Akihisa OsakabeGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Zdravko J LorkovicGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Wataru KobayashiGraduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
Hiroaki TachiwanaGraduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
Ramesh YelagandulaGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Hitoshi KurumizakaGraduate School of Advanced Science and Engineering, Waseda University, 2-2 Wakamatsu-cho, Shinjuku-ku, Tokyo 162-8480, Japan.
Frédéric BergerGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Austrian Academy of Sciences · ATWaseda University · JP

Funding

Austrian Science Fund FWF M 2539Austrian Science Fund FWF P 26887Austrian Science Fund FWF P 28320
6 · The paper itself

Abstract

In eukaryotes, variants of core histone H2A are selectively incorporated in distinct functional domains of chromatin and are distinguished by conserved sequences of their C-terminal tail, the L1 loop and the docking domain, suggesting that each variant confers specific properties to the nucleosome. Chromatin of flowering plants contains four types of H2A variants, which biochemical properties have not been characterized. We report that in contrast with animals, in Arabidopsis thaliana H2A variants define only four major types of homotypic nucleosomes containing exclusively H2A, H2A.Z, H2A.X or H2A.W. In vitro assays show that the L1 loop and the docking domain confer distinct stability of the nucleosome. In vivo and in vitro assays suggest that the L1 loop and the docking domain cooperate with the C-terminal tail to regulate chromatin accessibility. Based on these findings we conclude that the type of H2A variant in the nucleosome impacts on its interaction with DNA and propose that H2A variants regulate the dynamics of chromatin accessibility. In plants, the predominance of homotypic nucleosomes with specific physical properties and their specific localization to distinct domains suggest that H2A variants play a dominant role in chromatin dynamics and function.

Indexed as

Amino Acid SequenceAnimalsArabidopsis ProteinsBinding SitesChromatinDNAGenetic VariationHistonesHumansNucleosomesPlants, Genetically ModifiedProtein BindingProtein IsoformsSequence Homology, Amino AcidArabidopsis ProteinsChromatinDNAHistonesNucleosomesProtein Isoforms

Identifiers

PMID29945241
PMCPMC6125630
OpenAlexW2811489616

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.