Evidence map›Paper›PMID 31837996›Full record

ArticleMolecular cell2020

The Chaperone FACT and Histone H2B Ubiquitination Maintain S. pombe Genome Architecture through Genic and Subtelomeric Functions.

Magdalena Murawska, Tamas Schauer, Atsushi Matsuda, Marcus D Wilson, Thomas Pysik, Felix Wojcik, Tom W Muir, Yasushi Hiraoka, Tobias Straub, Andreas G Ladurner

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-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

32 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Paf1 complex subunit Rtf1 stimulates H2B ubiquitylation by interacting with the highly conserved N-terminal helix of Rad6.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Decoding histone ubiquitylation.Frontiers in cell and developmental biology · 2022
    Review
  19. Article
  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

10 authors at 4 institutions in 4 countries.

Magdalena MurawskaBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-University of Munich, 82152 Planegg-Martinsried, Germany.
Tamas SchauerBiomedical Center, Bioinformatics Unit, Ludwig-Maximilians-University of Munich, 82152 Planegg-Martinsried, Germany.
Atsushi MatsudaAdvanced ICT Research Institute Kobe, National Institute of Information and Communications Technology, 588-2 Iwaoka, Iwaoka-cho, Nishi-ku, Kobe 651-2492, Japan; Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita 565-0871, Japan.
Marcus D WilsonWellcome Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Kings Buildings, Mayfield Road, Edinburgh EH9 3JR, UK.
Thomas PysikBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-University of Munich, 82152 Planegg-Martinsried, Germany.
Felix WojcikDepartment of Chemistry, Princeton University, Princeton, NJ 08544, USA.
Tom W MuirDepartment of Chemistry, Princeton University, Princeton, NJ 08544, USA.
Yasushi HiraokaAdvanced ICT Research Institute Kobe, National Institute of Information and Communications Technology, 588-2 Iwaoka, Iwaoka-cho, Nishi-ku, Kobe 651-2492, Japan; Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita 565-0871, Japan.
Tobias StraubBiomedical Center, Bioinformatics Unit, Ludwig-Maximilians-University of Munich, 82152 Planegg-Martinsried, Germany.
Andreas G LadurnerBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-University of Munich, 82152 Planegg-Martinsried, Germany. Electronic address: andreas.ladurner@bmc.med.lmu.de.
Ludwig-Maximilians-Universität München · DEOsaka University · JPPrinceton University · USWellcome Centre for Cell Biology · GB

Funding

Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
Development and Applications of 'Designer Chromatin'R01GM107047 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2013 to 2016
$1.2M
NCI NIH HHS P01 CA196539NIGMS NIH HHS R01 GM107047NIGMS NIH HHS R37 GM086868Wellcome Trust
6 · The paper itself

Abstract

The histone chaperone FACT and histone H2B ubiquitination (H2Bub) facilitate RNA polymerase II (Pol II) passage through chromatin, yet it is not clear how they cooperate mechanistically. We used genomics, genetic, biochemical, and microscopic approaches to dissect their interplay in Schizosaccharomyces pombe. We show that FACT and H2Bub globally repress antisense transcripts near the 5' end of genes and inside gene bodies, respectively. The accumulation of these transcripts is accompanied by changes at genic nucleosomes and Pol II redistribution. H2Bub is required for FACT activity in genic regions. In the H2Bub mutant, FACT binding to chromatin is altered and its association with histones is stabilized, which leads to the reduction of genic nucleosomes. Interestingly, FACT depletion globally restores nucleosomes in the H2Bub mutant. Moreover, in the absence of Pob3, the FACT Spt16 subunit controls the 3' end of genes. Furthermore, FACT maintains nucleosomes in subtelomeric regions, which is crucial for their compaction.

Indexed as

ChromatinDNA-Binding ProteinsHigh Mobility Group ProteinsHistonesMolecular ChaperonesNucleosomesProtein BindingRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsTranscriptional Elongation FactorsTranscription FactorsUbiquitinationChromatinDNA-Binding ProteinsFACT protein, S cerevisiaeHigh Mobility Group ProteinsHistonesMolecular ChaperonesNucleosomesPOB3 protein, S cerevisiaeRNA Polymerase IISaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSPT16 protein, S cerevisiaeTranscriptional Elongation FactorsTranscription Factorschromatin structureFACTH2B ubiquitinationhistone chaperoneS. pombe

Identifiers

PMID31837996
PMCPMC7007867
OpenAlexW2994672877

What OpenQuestion holds

Textmetadata
LicenceTDM
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.