Evidence map›Paper›PMID 39270644›Full record

ArticleMolecular cell2024

Resolution of transcription-induced hexasome-nucleosome complexes by Chd1 and FACT.

Maik Engeholm, Johann J Roske, Elisa Oberbeckmann, Christian Dienemann, Michael Lidschreiber, Patrick Cramer, Lucas Farnung

Abstract read
In one paragraph

Article in Molecular cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Molecular Acrobats: How CHD Remodelers Shape the Genetic Playground to License Cell Identity.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Beyond the mono-nucleosome.Biochemical Society transactions · 2025
    Review
  15. Article
  16. Review
  17. Toward structural understanding of eukaryotic transcription elongation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
    Review
  18. RNA Polymerase II coordinates histone deacetylation at active promoters.bioRxiv : the preprint server for biology · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Maik EngeholmMax Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany. Electronic address: maik.engeholm@mpinat.mpg.de.
Johann J RoskeMax Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany; MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Elisa OberbeckmannMax Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.
Christian DienemannMax Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.
Michael LidschreiberMax Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany.
Patrick CramerMax Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany. Electronic address: patrick.cramer@mpinat.mpg.de.
Lucas FarnungMax Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen 37077, Germany; Harvard Medical School, Blavatnik Institute, Department of Cell Biology, 240 Longwood Avenue, Boston, MA 02115, USA. Electronic address: lucas_farnung@hms.harvard.edu.

Funding

Visualizing mechanisms at the intersection of chromatin, transcription, and epigeneticsDP2ES036404 · NIEHS · HARVARD MEDICAL SCHOOL · PI Lucas Farnung · 2023 to 2026
$2.5M
NIEHS NIH HHS DP2 ES036404
6 · The paper itself

Abstract

To maintain the nucleosome organization of transcribed genes, ATP-dependent chromatin remodelers collaborate with histone chaperones. Here, we show that at the 5' ends of yeast genes, RNA polymerase II (RNAPII) generates hexasomes that occur directly adjacent to nucleosomes. The resulting hexasome-nucleosome complexes are then resolved by Chd1. We present two cryoelectron microscopy (cryo-EM) structures of Chd1 bound to a hexasome-nucleosome complex before and after restoration of the missing inner H2A/H2B dimer by FACT. Chd1 uniquely interacts with the complex, positioning its ATPase domain to shift the hexasome away from the nucleosome. In the absence of the inner H2A/H2B dimer, its DNA-binding domain (DBD) packs against the ATPase domain, suggesting an inhibited state. Restoration of the dimer by FACT triggers a rearrangement that displaces the DBD and stimulates Chd1 remodeling. Our results demonstrate how chromatin remodelers interact with a complex nucleosome assembly and suggest how Chd1 and FACT jointly support transcription by RNAPII.

Indexed as

Chromatin Assembly and DisassemblyCryoelectron MicroscopyDNA-Binding ProteinsHigh Mobility Group ProteinsHistonesNucleosomesRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsTranscription, GeneticAdenosine TriphosphatasesModels, MolecularProtein BindingAdenosine TriphosphatasesCHD1 protein, S cerevisiaeDNA-Binding ProteinsFACT protein, S cerevisiaeHigh Mobility Group ProteinsHistonesNucleosomesRNA Polymerase IISaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsChd1chromatin remodelingFACThexasome-nucleosome complexestranscription

Identifiers

PMID39270644
PMCPMC11441371

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Registered trials

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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.