Evidence map›Paper›PMID 30177554›Full record

ArticleEMBO reports2018

MacroH2A histone variants limit chromatin plasticity through two distinct mechanisms.

Marek Kozlowski, David Corujo, Michael Hothorn, Iva Guberovic, Imke K Mandemaker, Charlotte Blessing, Judith Sporn, Arturo Gutierrez-Triana, Rebecca Smith, Thomas Portmann and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.4field-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

49 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Epigenetic Regulation in Lean Nonalcoholic Fatty Liver Disease.International journal of molecular sciences · 2023
    Review
  18. Article
  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

16 authors at 5 institutions in 3 countries.

Marek KozlowskiBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
David CorujoJosep Carreras Leukaemia Research Institute, Campus ICO-Germans Trias i Pujol, Universitat Autònoma de Barcelona, Badalona, Spain.
Michael HothornEuropean Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0002-3597-5698
Iva GuberovicJosep Carreras Leukaemia Research Institute, Campus ICO-Germans Trias i Pujol, Universitat Autònoma de Barcelona, Badalona, Spain.
Imke K MandemakerBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
Charlotte BlessingBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
Judith SpornEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Arturo Gutierrez-TrianaEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Rebecca SmithBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
Thomas PortmannEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Mathias TreierEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Klaus ScheffzekEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Sebastien HuetUniv Rennes, CNRS, Structure fédérative de recherche Biosit, IGDR (Institut de génétique et développement de Rennes) - UMR 6290, Rennes, France.
Gyula TiminszkyBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.ORCID 0000-0001-6342-8985
Marcus BuschbeckJosep Carreras Leukaemia Research Institute, Campus ICO-Germans Trias i Pujol, Universitat Autònoma de Barcelona, Badalona, Spain mbuschbeck@carrerasresearch.org andreas.ladurner@bmc.med.lmu.de.ORCID 0000-0002-3218-4567
Andreas G LadurnerBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany mbuschbeck@carrerasresearch.org andreas.ladurner@bmc.med.lmu.de.ORCID 0000-0003-3835-232X
European Molecular Biology Laboratory · DELudwig-Maximilians-Universität München · DEUniversitat Autònoma de Barcelona · ESCenter for Integrated Protein Science Munich · DECentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MacroH2A histone variants suppress tumor progression and act as epigenetic barriers to induced pluripotency. How they impart their influence on chromatin plasticity is not well understood. Here, we analyze how the different domains of macroH2A proteins contribute to chromatin structure and dynamics. By solving the crystal structure of the macrodomain of human macroH2A2 at 1.7 Å, we find that its putative binding pocket exhibits marked structural differences compared with the macroH2A1.1 isoform, rendering macroH2A2 unable to bind ADP-ribose. Quantitative binding assays show that this specificity is conserved among vertebrate macroH2A isoforms. We further find that macroH2A histones reduce the transient, PARP1-dependent chromatin relaxation that occurs in living cells upon DNA damage through two distinct mechanisms. First, macroH2A1.1 mediates an isoform-specific effect through its ability to suppress PARP1 activity. Second, the unstructured linker region exerts an additional repressive effect that is common to all macroH2A proteins. In the absence of DNA damage, the macroH2A linker is also sufficient for rescuing heterochromatin architecture in cells deficient for macroH2A.

Indexed as

Adenosine Diphosphate RiboseChromatinCrystallography, X-RayDNA DamageEpigenesis, GeneticHeterochromatinHistonesHumansPoly (ADP-Ribose) Polymerase-1Protein ConformationProtein IsoformsAdenosine Diphosphate RiboseChromatinHeterochromatinHistonesmacroH2A histonePoly (ADP-Ribose) Polymerase-1Protein IsoformsDNA damageheterochromatinhistone variantsmacroH2APARP1

Identifiers

PMID30177554
PMCPMC6172464
OpenAlexW2889323361

What OpenQuestion holds

Textmetadata
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.