Evidence map›Paper›PMID 34731638›Full record

ArticleCell reports2021

The histone chaperone FACT facilitates heterochromatin spreading by regulating histone turnover and H3K9 methylation states.

Magdalena Murawska, R A Greenstein, Tamas Schauer, Karl C F Olsen, Henry Ng, Andreas G Ladurner, Bassem Al-Sady, Sigurd Braun

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  13. Specialized replication of heterochromatin domains ensures self-templated chromatin assembly and epigenetic inheritance.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Facilitates Chromatin Transcription in Breast and Other Cancers.Advances in experimental medicine and biology · 2024
    Review
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  17. Review
  18. Article
  19. Review
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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

8 authors at 4 institutions in 2 countries.

Magdalena MurawskaPhysiological Chemistry, Biomedical Center, Faculty of Medicine, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany. Electronic address: magdalena.murawska@bmc.med.lmu.de.
R A GreensteinDepartment of Microbiology and Immunology, University of California, San Francisco, CA 94143, USA; George Williams Hooper Research Foundation, University of California, San Francisco, CA 94143, USA; TETRAD Graduate Program, University of California, San Francisco, CA 94143, USA.
Tamas SchauerBioinformatics Unit, Biomedical Center, Faculty of Medicine, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany.
Karl C F OlsenPhysiological Chemistry, Biomedical Center, Faculty of Medicine, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany; International Max Planck Research School for Molecular and Cellular Life Sciences, 82152 Planegg-Martinsried, Germany.
Henry NgDepartment of Microbiology and Immunology, University of California, San Francisco, CA 94143, USA; George Williams Hooper Research Foundation, University of California, San Francisco, CA 94143, USA; TETRAD Graduate Program, University of California, San Francisco, CA 94143, USA.
Andreas G LadurnerPhysiological Chemistry, Biomedical Center, Faculty of Medicine, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany; International Max Planck Research School for Molecular and Cellular Life Sciences, 82152 Planegg-Martinsried, Germany.
Bassem Al-SadyDepartment of Microbiology and Immunology, University of California, San Francisco, CA 94143, USA; George Williams Hooper Research Foundation, University of California, San Francisco, CA 94143, USA. Electronic address: bassem.al-sady@ucsf.edu.
Sigurd BraunPhysiological Chemistry, Biomedical Center, Faculty of Medicine, Ludwig-Maximilians-University Munich, 82152 Planegg-Martinsried, Germany; International Max Planck Research School for Molecular and Cellular Life Sciences, 82152 Planegg-Martinsried, Germany; Institute for Genetics, Justus-Liebig University Giessen, 35392 Giessen, Germany. Electronic address: sigurd.braun@gen.bio.uni-giessen.de.
University of California, San Francisco · USLudwig-Maximilians-Universität München · DEMax Planck Institute of Biochemistry · DEJustus-Liebig-Universität Gießen · DE

Funding

Reconstructing dynamic epigenetic genome partitioning in single stem cellsDP2GM123484 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AL-SADY, BASSEM · 2016 to 2020
$2.5M
Tracking how molecular machines propagate epigenetic information in time and spaceR35GM141888 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI AL-SADY, BASSEM · 2021 to 2025
$2.3M
NIGMS NIH HHS DP2 GM123484NIGMS NIH HHS R35 GM141888
6 · The paper itself

Abstract

Heterochromatin formation requires three distinct steps: nucleation, self-propagation (spreading) along the chromosome, and faithful maintenance after each replication cycle. Impeding any of those steps induces heterochromatin defects and improper gene expression. The essential histone chaperone FACT (facilitates chromatin transcription) has been implicated in heterochromatin silencing, but the mechanisms by which FACT engages in this process remain opaque. Here, we pinpoint its function to the heterochromatin spreading process in fission yeast. FACT impairment reduces nucleation-distal H3K9me3 and HP1/Swi6 accumulation at subtelomeres and derepresses genes in the vicinity of heterochromatin boundaries. FACT promotes spreading by repressing heterochromatic histone turnover, which is crucial for the H3K9me2 to me3 transition that enables spreading. FACT mutant spreading defects are suppressed by removal of the H3K9 methylation antagonist Epe1. Together, our study identifies FACT as a histone chaperone that promotes heterochromatin spreading and lends support to the model that regulated histone turnover controls the propagation of repressive methylation marks.

Indexed as

Chromatin Assembly and DisassemblyProtein Processing, Post-TranslationalAminopeptidasesCell Cycle ProteinsGene Expression Regulation, FungalGene SilencingHeterochromatinHistone ChaperonesHistone-Lysine N-MethyltransferaseHistonesMethylationMutationNuclear ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsTranscription, GeneticAminopeptidasesCell Cycle Proteinsclr4 protein, S pombeepe1 protein, S pombeHeterochromatinHistone ChaperonesHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsSchizosaccharomyces pombe ProteinsSpt16 protein, S pombeEpe1FACTheterochromatin spreadinghistone chaperonehistone turnover

Identifiers

PMID34731638
PMCPMC8608617
OpenAlexW3211011193

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.