Evidence map›Paper›PMID 30239791›Full record

ReviewNucleic acids research2018

Mechanistic insights into histone deposition and nucleosome assembly by the chromatin assembly factor-1.

Paul V Sauer, Yajie Gu, Wallace H Liu, Francesca Mattiroli, Daniel Panne, Karolin Luger, Mair Ea Churchill

Open access · goldAbstract readReview
In one paragraph

Review in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
2.9field-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

59 citing papers in PubMed, 92 citations in OpenAlex.

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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

7 authors at 6 institutions in 4 countries.

Paul V SauerEuropean Molecular Biology Laboratory, 38042 Grenoble, France.
Yajie GuDepartment of Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.
Wallace H LiuDepartment of Pharmacology, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
Francesca MattiroliHubrecht Institute, Utrecht 3584 CT, the Netherlands.
Daniel PanneEuropean Molecular Biology Laboratory, 38042 Grenoble, France.
Karolin LugerDepartment of Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.
Mair Ea ChurchillDepartment of Pharmacology and Program in Structural Biology and Biochemistry, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
University of Colorado Anschutz Medical Campus · USEuropean Molecular Biology Laboratory · FRHoward Hughes Medical Institute · USHubrecht Institute for Developmental Biology and Stem Cell Research · NLUniversity of Colorado Boulder · USUniversity of Leicester · GB

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Scott Kopetz · 1985 to 2026
$290.8M
University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
Structural and Functional Studies of the Histone Chaperone CAF-1R01GM111902 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI CHURCHILL, MAIR E · 2014 to 2017
$1.2M
NCI NIH HHS P30 CA046934NIGMS NIH HHS R01 GM111902
6 · The paper itself

Abstract

Eukaryotic chromatin is a highly dynamic structure with essential roles in virtually all DNA-dependent cellular processes. Nucleosomes are a barrier to DNA access, and during DNA replication, they are disassembled ahead of the replication machinery (the replisome) and reassembled following its passage. The Histone chaperone Chromatin Assembly Factor-1 (CAF-1) interacts with the replisome and deposits H3-H4 directly onto newly synthesized DNA. Therefore, CAF-1 is important for the establishment and propagation of chromatin structure. The molecular mechanism by which CAF-1 mediates H3-H4 deposition has remained unclear. However, recent studies have revealed new insights into the architecture and stoichiometry of the trimeric CAF-1 complex and how it interacts with and deposits H3-H4 onto substrate DNA. The CAF-1 trimer binds to a single H3-H4 dimer, which induces a conformational rearrangement in CAF-1 promoting its interaction with substrate DNA. Two CAF-1•H3-H4 complexes co-associate on nucleosome-free DNA depositing (H3-H4)2 tetramers in the first step of nucleosome assembly. Here, we review the progress made in our understanding of CAF-1 structure, mechanism of action, and how CAF-1 contributes to chromatin dynamics during DNA replication.

Indexed as

AnimalsChromatinChromatin Assembly and DisassemblyChromatin Assembly Factor-1HistonesHumansMolecular ChaperonesNucleosomesChromatinChromatin Assembly Factor-1HistonesMolecular ChaperonesNucleosomes

Identifiers

PMID30239791
PMCPMC6212844
OpenAlexW2892187207

What OpenQuestion holds

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LicenceCC BY-NC
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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.