Evidence map›Paper›PMID 30217558›Full record

ArticleMolecular cell2018

POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication.

Roberto Bellelli, Ondrej Belan, Valerie E Pye, Camille Clement, Sarah L Maslen, J Mark Skehel, Peter Cherepanov, Genevieve Almouzni, Simon J Boulton

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

85 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. HAT1 Regulates Intestinal Stem Cell Proliferation and Differentiation.bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Characterizing the Ovarian Cytogenetic Dynamics of Sichuan Bream (International journal of molecular sciences · 2025
    Article
  18. Article
  19. Article
  20. Review

25 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 2 countries.

Roberto BellelliThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Ondrej BelanThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Valerie E PyeThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Camille ClementInstitut Curie, PSL Research University, CNRS, UMR3664, Equipe Labellisée Ligue contre le Cancer, Paris, France; Sorbonne Universités, UPMC Univ Paris 06, CNRS, UMR3664, Paris, France.
Sarah L MaslenMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.
J Mark SkehelMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.
Peter CherepanovThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Genevieve AlmouzniInstitut Curie, PSL Research University, CNRS, UMR3664, Equipe Labellisée Ligue contre le Cancer, Paris, France; Sorbonne Universités, UPMC Univ Paris 06, CNRS, UMR3664, Paris, France.
Simon J BoultonThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK. Electronic address: simon.boulton@crick.ac.uk.
The Francis Crick Institute · GBCentre National de la Recherche Scientifique · FRMRC Laboratory of Molecular Biology · GB

Funding

Cancer Research UK FC0010048Medical Research Council FC0010048Wellcome TrustWellcome Trust FC0010048
6 · The paper itself

Abstract

Maintenance of epigenetic integrity relies on coordinated recycling and partitioning of parental histones and deposition of newly synthesized histones during DNA replication. This process depends upon a poorly characterized network of histone chaperones, remodelers, and binding proteins. Here we implicate the POLE3-POLE4 subcomplex of the leading-strand polymerase, Polε, in replication-coupled nucleosome assembly through its ability to selectively bind to histones H3-H4. Using hydrogen/deuterium exchange mass spectrometry and physical mapping, we define minimal domains necessary for interaction between POLE3-POLE4 and histones H3-H4. Biochemical analyses establish that POLE3-POLE4 is a histone chaperone that promotes tetrasome formation and DNA supercoiling in vitro. In cells, POLE3-POLE4 binds both newly synthesized and parental histones, and its depletion hinders helicase unwinding and chromatin PCNA unloading and compromises coordinated parental histone retention and new histone deposition. Collectively, our study reveals that POLE3-POLE4 possesses intrinsic H3-H4 chaperone activity, which facilitates faithful nucleosome dynamics at the replication fork.

Indexed as

ChromatinDNA-Binding ProteinsDNA Polymerase IIDNA Polymerase IIIDNA ReplicationEpigenesis, GeneticHistone ChaperonesHistonesHumansMolecular ChaperonesNucleoproteinsNucleosomesPoly-ADP-Ribose Binding ProteinsProliferating Cell Nuclear AntigenProtein BindingChromatinDNA-Binding ProteinsDNA Polymerase IIDNA Polymerase IIIHistone ChaperonesHistonesMolecular ChaperonesNucleoproteinsNucleosomesPOLE3 protein, humanPOLE protein, humanPoly-ADP-Ribose Binding ProteinsProliferating Cell Nuclear Antigenepigenome stabilityhistone chaperonePOLE3-POLE4 complexreplication-coupled nucleosome assembly

Identifiers

PMID30217558
PMCPMC6179962
OpenAlexW2890968295

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.