Evidence map›Paper›PMID 28315525›Full record

ArticleeLife2017

Insights into the molecular architecture and histone H3-H4 deposition mechanism of yeast Chromatin assembly factor 1.

Paul Victor Sauer, Jennifer Timm, Danni Liu, David Sitbon, Elisabetta Boeri-Erba, Christophe Velours, Norbert Mücke, Jörg Langowski, Françoise Ochsenbein, Geneviève Almouzni and 1 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 66 citations in OpenAlex.

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  15. Acute multi-level response to defectivebioRxiv : the preprint server for biology · 2024
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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

11 authors at 5 institutions in 2 countries.

Paul Victor SauerEuropean Molecular Biology Laboratory, Grenoble, France.ORCID 0000-0001-7204-5863
Jennifer TimmEuropean Molecular Biology Laboratory, Grenoble, France.
Danni LiuCEA, DRF, SB2SM, Laboratoire de Biologie Structurale et Radiobiologie, Gif-sur-Yvette, France.
David SitbonInstitut Curie, PSL Research University, CNRS, UMR3664, Equipe Labellisée Ligue contre le Cancer, Paris, France.
Elisabetta Boeri-ErbaUniversité Grenoble Alpes, Institut de Biologie Structurale (IBS), Grenoble, France.
Christophe VeloursInstitute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, France.
Norbert MückeAbteilung Biophysik der Makromoleküle, Deutsches Krebsforschungszentrum, Heidelberg, Germany.
Jörg LangowskiAbteilung Biophysik der Makromoleküle, Deutsches Krebsforschungszentrum, Heidelberg, Germany.
Françoise OchsenbeinCEA, DRF, SB2SM, Laboratoire de Biologie Structurale et Radiobiologie, Gif-sur-Yvette, France.
Geneviève AlmouzniInstitut Curie, PSL Research University, CNRS, UMR3664, Equipe Labellisée Ligue contre le Cancer, Paris, France.
Daniel PanneEuropean Molecular Biology Laboratory, Grenoble, France.ORCID 0000-0001-9158-5507
European Molecular Biology Laboratory · FRUniversité Paris-Sud · FRCentre National de la Recherche Scientifique · FRGerman Cancer Research Center · DECommissariat à l'Énergie Atomique et aux Énergies Alternatives · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

How the very first step in nucleosome assembly, deposition of histone H3-H4 as tetramers or dimers on DNA, is accomplished remains largely unclear. Here, we report that yeast chromatin assembly factor 1 (CAF1), a conserved histone chaperone complex that deposits H3-H4 during DNA replication, binds a single H3-H4 heterodimer in solution. We identify a new DNA-binding domain in the large Cac1 subunit of CAF1, which is required for high-affinity DNA binding by the CAF1 three-subunit complex, and which is distinct from the previously described C-terminal winged-helix domain. CAF1 binds preferentially to DNA molecules longer than 40 bp, and two CAF1-H3-H4 complexes concertedly associate with DNA molecules of this size, resulting in deposition of H3-H4 tetramers. While DNA binding is not essential for H3-H4 tetrasome deposition in vitro, it is required for efficient DNA synthesis-coupled nucleosome assembly. Mutant histones with impaired H3-H4 tetramerization interactions fail to release from CAF1, indicating that DNA deposition of H3-H4 tetramers by CAF1 requires a hierarchical cooperation between DNA binding, H3-H4 deposition and histone tetramerization.

Indexed as

DNA, FungalDNA ReplicationHistonesProtein BindingProtein MultimerizationRibonucleasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA, FungalHistonesPOP2 protein, S cerevisiaeRibonucleasesSaccharomyces cerevisiae Proteinsbiochemistrybiophysicschromatinchromatin assembly factor 1DNA replicationhistone chaperonehistonesS. cerevisiaestructural biology

Identifiers

PMID28315525
PMCPMC5404918
OpenAlexW2595480511

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.