Evidence map›Paper›PMID 22941638›Full record

ArticleNucleic acids research2012

Yeast CAF-1 assembles histone (H3-H4)2 tetramers prior to DNA deposition.

Duane D Winkler, Hui Zhou, Mohd A Dar, Zhiguo Zhang, Karolin Luger

RetractedOpen access · goldAbstract readRetracted Publication
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.6field-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

53 citing papers in PubMed, 78 citations in OpenAlex.

  1. HAT1 Regulates Intestinal Stem Cell Proliferation and Differentiation.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Unorthodox PCNA Binding by Chromatin Assembly Factor 1.International journal of molecular sciences · 2022
    Article
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  20. Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Duane D WinklerHoward Hughes Medical Institute and the Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523, USA.
Hui Zhou
Mohd A Dar
Zhiguo Zhang
Karolin Luger
Colorado State University · USMayo Clinic · USHoward Hughes Medical Institute · US

Funding

Targeted MV-CEA as a Potent Antitumor Agent against GBMP50CA108961 · NCI · MAYO CLINIC ROCHESTER · PI O'NEILL, BRIAN PATRICK · 2004 to 2015
$22.5M
Structure and Function of Nucleosome Assembly Protein 1R01GM067777 · NIGMS · UNIVERSITY OF COLORADO · PI LUGER, KAROLIN · 2003 to 2015
$3.7M
Histone chaperones and transcriptional silencingR01GM072719 · NIGMS · MAYO CLINIC ROCHESTER · PI ZHANG, ZHIGUO · 2005 to 2015
$2.9M
Structural and Mechanistic Characterization of the Histone Chaperone FACTF32GM096531 · NIGMS · COLORADO STATE UNIVERSITY · PI WINKLER, DUANE DAVID · 2011 to 2012
$101k
Howard Hughes Medical InstituteNCI NIH HHS P50 CA108961NIGMS NIH HHS F32GM096531NIGMS NIH HHS GM- 067777NIGMS NIH HHS GM72719NIGMS NIH HHS R01 GM072719
6 · The paper itself

Abstract

Following acetylation, newly synthesized H3-H4 is directly transferred from the histone chaperone anti-silencing factor 1 (Asf1) to chromatin assembly factor 1 (CAF-1), another histone chaperone that is critical for the deposition of H3-H4 onto replicating DNA. However, it is unknown how CAF-1 binds and delivers H3-H4 to the DNA. Here, we show that CAF-1 binds recombinant H3-H4 with 10- to 20-fold higher affinity than H2A-H2B in vitro, and H3K56Ac increases the binding affinity of CAF-1 toward H3-H4 2-fold. These results provide a quantitative thermodynamic explanation for the specific H3-H4 histone chaperone activity of CAF-1. Surprisingly, H3-H4 exists as a dimer rather than as a canonical tetramer at mid-to-low nanomolar concentrations. A single CAF-1 molecule binds a cross-linked (H3-H4)2 tetramer, or two H3-H4 dimers that contain mutations at the (H3-H4)2 tetramerization interface. These results suggest that CAF-1 binds to two H3-H4 dimers in a manner that promotes formation of a (H3-H4)2 tetramer. Consistent with this idea, we confirm that CAF-1 synchronously binds two H3-H4 dimers derived from two different histone genes in vivo. Together, the data illustrate a clear mechanism for CAF-1-associated H3-H4 chaperone activity in the context of de novo nucleosome (re)assembly following DNA replication.

Indexed as

AcetylationAnimalsChromatin Assembly Factor-1DNAFungal ProteinsHistonesProtein BindingProtein MultimerizationSequence DeletionThermodynamicsXenopus laevisYeastsChromatin Assembly Factor-1DNAFungal ProteinsHistones

Identifiers

PMID22941638
PMCPMC3488248
OpenAlexW2098521000

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.