Evidence map›Paper›PMID 31308435›Full record

ArticleScientific reports2019

Structural visualization of key steps in nucleosome reorganization by human FACT.

Kouta Mayanagi, Kazumi Saikusa, Naoyuki Miyazaki, Satoko Akashi, Kenji Iwasaki, Yoshifumi Nishimura, Kosuke Morikawa, Yasuo Tsunaka

Abstract read
In one paragraph

Article in Scientific reports, 2019. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Beyond Chaperoning: The Multifaceted Role of FACT in Chromatin Transactions.International journal of molecular sciences · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Structural advances in transcription elongation.Current opinion in structural biology · 2022
    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

8 authors.

Kouta MayanagiMedical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka-shi, Fukuoka, 812-8582, Japan. maya@bioreg.kyushu-u.ac.jp.
Kazumi SaikusaGraduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima, Hiroshima, 739-8526, Japan.ORCID http://orcid.org/0000-0003-4135-2048
Naoyuki MiyazakiLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Satoko AkashiGraduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan.ORCID http://orcid.org/0000-0002-8978-6358
Kenji IwasakiLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.ORCID http://orcid.org/0000-0002-3808-8904
Yoshifumi NishimuraGraduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan.ORCID http://orcid.org/0000-0002-5148-3458
Kosuke MorikawaDepartment of Gene Mechanisms, Graduate School of Biostudies, Kyoto University, Yoshida-konoemachi, Sakyo-ku, Kyoto, 606-8501, Japan. morikawa.kosuke.2@kyoto-u.ac.jp.
Yasuo TsunakaGraduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan. tsunaka@yokohama-cu.ac.jp.ORCID http://orcid.org/0000-0002-7366-7610

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Facilitates chromatin transcription (FACT) is a histone chaperone, which accomplishes both nucleosome assembly and disassembly. Our combined cryo-electron microscopy (EM) and native mass spectrometry (MS) studies revealed novel key steps of nucleosome reorganization conducted by a Mid domain and its adjacent acidic AID segment of human FACT. We determined three cryo-EM structures of respective octasomes complexed with the Mid-AID and AID regions, and a hexasome alone. We discovered extensive contacts between a FACT region and histones H2A, H2B, and H3, suggesting that FACT is competent to direct functional replacement of a nucleosomal DNA end by its phosphorylated AID segment (pAID). Mutational assays revealed that the aromatic and phosphorylated residues within pAID are essential for octasome binding. The EM structure of the hexasome, generated by the addition of Mid-pAID or pAID, indicated that the dissociation of H2A-H2B dimer causes significant alteration from the canonical path of the nucleosomal DNA.

Indexed as

ChromatinChromatin Assembly and DisassemblyCryoelectron MicroscopyDNADNA-Binding ProteinsHigh Mobility Group ProteinsHistonesHumansMass SpectrometryModels, MolecularMolecular ChaperonesNucleosomesProtein BindingTranscriptional Elongation FactorsChromatinDNADNA-Binding ProteinsHigh Mobility Group ProteinsHistonesMolecular ChaperonesNucleosomesSSRP1 protein, humanTranscriptional Elongation Factors

Identifiers

PMID31308435
PMCPMC6629675

What OpenQuestion holds

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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.