Evidence map›Paper›PMID 22467210›Full record

ArticleNucleic acids research2012

H2A.Z.2.2 is an alternatively spliced histone H2A.Z variant that causes severe nucleosome destabilization.

Clemens Bönisch, Katrin Schneider, Sebastian Pünzeler, Sonja M Wiedemann, Christina Bielmeier, Marco Bocola, H Christian Eberl, Wolfgang Kuegel, Jürgen Neumann, Elisabeth Kremmer and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
4.2field-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

67 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Basic Epigenetic Mechanisms.Sub-cellular biochemistry · 2025
    Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Histone H2A variants: Diversifying chromatin to ensure genome integrity.Seminars in cell & developmental biology · 2023
    Review
  16. Article
  17. Article
  18. Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023
    Review
  19. Characterization of the B-Cell Epitopes ofFrontiers in cellular and infection microbiology · 2022
    Article
  20. Review

7 more citing papers are in PubMed but not listed here.

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

15 authors at 3 institutions in 2 countries.

Clemens BönischDepartment of Molecular Biology, Adolf-Butenandt-Institute, Ludwig-Maximilians-University Munich, 80336 Munich, Germany.
Katrin Schneider
Sebastian Pünzeler
Sonja M Wiedemann
Christina Bielmeier
Marco Bocola
H Christian Eberl
Wolfgang Kuegel
Jürgen Neumann
Elisabeth Kremmer
Heinrich Leonhardt
Matthias Mann
Jens Michaelis
Lothar Schermelleh
Sandra B Hake
Center for Integrated Protein Science Munich · DEMax Planck Society · DELudwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The histone variant H2A.Z has been implicated in many biological processes, such as gene regulation and genome stability. Here, we present the identification of H2A.Z.2.2 (Z.2.2), a novel alternatively spliced variant of histone H2A.Z and provide a comprehensive characterization of its expression and chromatin incorporation properties. Z.2.2 mRNA is found in all human cell lines and tissues with highest levels in brain. We show the proper splicing and in vivo existence of this variant protein in humans. Furthermore, we demonstrate the binding of Z.2.2 to H2A.Z-specific TIP60 and SRCAP chaperone complexes and its active replication-independent deposition into chromatin. Strikingly, various independent in vivo and in vitro analyses, such as biochemical fractionation, comparative FRAP studies of GFP-tagged H2A variants, size exclusion chromatography and single molecule FRET, in combination with in silico molecular dynamics simulations, consistently demonstrate that Z.2.2 causes major structural changes and significantly destabilizes nucleosomes. Analyses of deletion mutants and chimeric proteins pinpoint this property to its unique C-terminus. Our findings enrich the list of known human variants by an unusual protein belonging to the H2A.Z family that leads to the least stable nucleosome known to date.

Indexed as

Alternative SplicingAdenosine TriphosphatasesCell LineChromatinDNAHistone AcetyltransferasesHistonesHumansLysine Acetyltransferase 5NucleosomesProtein IsoformsProtein Structure, TertiaryAdenosine TriphosphatasesChromatinDNAHistone Acetyltransferaseshistone H2A.F-ZHistonesKAT5 protein, humanLysine Acetyltransferase 5NucleosomesProtein IsoformsSRCAP protein, human

Identifiers

PMID22467210
PMCPMC3401452
OpenAlexW2147397612

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.