Evidence map›Paper›PMID 21447559›Full record

ArticleNucleic acids research2011

The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4-DNA complexes.

Douglas C Donham, Jean K Scorgie, Mair E A Churchill

Abstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
–field-weighted citation impact
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

43 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Mechanisms of chromatin-based epigenetic inheritance.Science China. Life sciences · 2022
    Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Interactions With Histone H3 & Tools to Study Them.Frontiers in cell and developmental biology · 2020
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017
    Review
  19. Article
  20. 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

3 authors.

Douglas C DonhamDepartment of Pharmacology, University of Colorado, School of Medicine, Aurora, CO 80045, USA.
Jean K Scorgie
Mair E A Churchill

Funding

Molecular Mechanism of Histone H3/H4 Chaperone FunctionR01GM079154 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI CHURCHILL, MAIR E · 2007 to 2010
$1.3M
NIGMS NIH HHS R01 GM079154
6 · The paper itself

Abstract

The deposition of the histones H3/H4 onto DNA to give the tetrasome intermediate and the displacement of H3/H4 from DNA are thought to be the first and the last steps in nucleosome assembly and disassembly, respectively. Anti-silencing function 1 (Asf1) is a chaperone of the H3/H4 dimer that functions in both of these processes. However, little is known about the thermodynamics of chaperone-histone interactions or the direct role of Asf1 in the formation or disassembly of histone-DNA complexes. Here, we show that Saccharomyces cerevisiae Asf1 shields H3/H4 from unfavorable DNA interactions and aids the formation of favorable histone-DNA interactions through the formation of disomes. However, Asf1 was unable to disengage histones from DNA for tetrasomes formed with H3/H4 and strong nucleosome positioning DNA sequences or tetrasomes weakened by mutant (H3K56Q/H4) histones or non-positioning DNA sequences. Furthermore, Asf1 did not associate with preformed tetrasomes. These results are consistent with the measured affinity of Asf1 for H3/H4 dimers of 2.5 nM, which is weaker than the association of H3/H4 for DNA. These studies support a mechanism by which Asf1 aids H3/H4 deposition onto DNA but suggest that additional factors or post-translational modifications are required for Asf1 to remove H3/H4 from tetrasome intermediates in chromatin.

Indexed as

AnimalsCell Cycle ProteinsDNAHistonesHMGB1 ProteinMolecular ChaperonesNucleosomesSaccharomyces cerevisiae ProteinsXenopus laevisASF1 protein, S cerevisiaeCell Cycle ProteinsDNAHistonesHMGB1 ProteinMolecular ChaperonesNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID21447559
PMCPMC3141235

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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.