Evidence map›Paper›PMID 30104407›Full record

ArticleThe EMBO journal2018

Histone H2A-H2B binding by Pol α in the eukaryotic replisome contributes to the maintenance of repressive chromatin.

Cecile Evrin, Joseph D Maman, Aurora Diamante, Luca Pellegrini, Karim Labib

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

52 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Four decades of Eukaryotic DNA replication: From yeast genetics to high-resolution cryo-EM structures of the replisome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. DNA polymerase delta governs parental histone transfer to DNA replication lagging strand.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Article
  20. Minimal requirements for the epigenetic inheritance of engineered silent chromatin domains.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

5 authors at 2 institutions in 1 country.

Cecile EvrinMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dundee, UK.
Joseph D MamanDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Aurora DiamanteDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Luca PellegriniDepartment of Biochemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-9300-497X
Karim LabibMRC Protein Phosphorylation and Ubiquitylation Unit, Sir James Black Centre, School of Life Sciences, University of Dundee, Dundee, UK kpmlabib@dundee.ac.uk.ORCID 0000-0001-8861-379X
University of Cambridge · GBUniversity of Dundee · GB

Funding

Medical Research Council MC_UU_00018/4Medical Research Council MC_UU_12016/13Wellcome Trust 102943/Z/13/ZWellcome Trust 104641/Z/14/Z
6 · The paper itself

Abstract

The eukaryotic replisome disassembles parental chromatin at DNA replication forks, but then plays a poorly understood role in the re-deposition of the displaced histone complexes onto nascent DNA. Here, we show that yeast DNA polymerase α contains a histone-binding motif that is conserved in human Pol α and is specific for histones H2A and H2B. Mutation of this motif in budding yeast cells does not affect DNA synthesis, but instead abrogates gene silencing at telomeres and mating-type loci. Similar phenotypes are produced not only by mutations that displace Pol α from the replisome, but also by mutation of the previously identified histone-binding motif in the CMG helicase subunit Mcm2, the human orthologue of which was shown to bind to histones H3 and H4. We show that chromatin-derived histone complexes can be bound simultaneously by Mcm2, Pol α and the histone chaperone FACT that is also a replisome component. These findings indicate that replisome assembly unites multiple histone-binding activities, which jointly process parental histones to help preserve silent chromatin during the process of chromosome duplication.

Indexed as

ChromatinDNA-Binding ProteinsDNA Polymerase IHigh Mobility Group ProteinsHistonesHumansSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsChromatinDNA-Binding ProteinsDNA Polymerase IFACT protein, S cerevisiaeHigh Mobility Group ProteinsHistonesMCM2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscriptional Elongation FactorsDNA polymerase alphaDNA replicationhistone chaperonehistonesreplisome

Identifiers

PMID30104407
PMCPMC6166128
OpenAlexW2885378257

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.