Evidence map›Paper›PMID 21969605›Full record

ArticleMolecular and cellular biology2011

Extranucleosomal DNA binding directs nucleosome sliding by Chd1.

Jeffrey N McKnight, Katherine R Jenkins, Ilana M Nodelman, Thelma Escobar, Gregory D Bowman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

80 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Structure and Function of Chromatin Remodelers.Journal of molecular biology · 2021
    Review
  19. Review
  20. Article

20 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Jeffrey N McKnightTC Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218-2685, USA.
Katherine R Jenkins
Ilana M Nodelman
Thelma Escobar
Gregory D Bowman
Johns Hopkins University · US

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Structural and Functional Characterization of the Chd1 Chromatin RemodelerR01GM084192 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BOWMAN, GREGORY DEAN · 2008 to 2024
$6.3M
Intramural NIH HHSNIGMS NIH HHS 2T32 GM008403-21NIGMS NIH HHS R01 GM084192NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

Chd1- and ISWI-type chromatin remodelers can sense extranucleosomal DNA and preferentially shift nucleosomes toward longer stretches of available DNA. The DNA-binding domains of these chromatin remodelers are believed to be responsible for sensing extranucleosomal DNA and are needed for robust sliding, but it is unclear how these domains contribute to directional movement of nucleosomes. Here, we show that the DNA-binding domain of Chd1 is not essential for nucleosome sliding but is critical for centering mononucleosomes on short DNA fragments. Remarkably, nucleosome centering was achieved by replacing the native DNA-binding domain of Chd1 with foreign DNA-binding domains of Escherichia coli AraC or Drosophila melanogaster engrailed. Introducing target DNA sequences recognized by the foreign domains enabled the remodelers to rapidly shift nucleosomes toward these binding sites, demonstrating that these foreign DNA-binding domains dictated the direction of sliding. Sequence-directed sliding occluded the target DNA sequences on the nucleosome enough to promote release of the remodeler. Target DNA sequences were highly stimulatory at multiple positions flanking the nucleosome and had the strongest influence when separated from the nucleosome by 23 or fewer base pairs. These results suggest that the DNA-binding domain's affinity for extranucleosomal DNA is the key determinant for the direction that Chd1 shifts the nucleosome.

Indexed as

Chromatin Assembly and DisassemblySaccharomyces cerevisiaeAdenosine TriphosphateAraC Transcription FactorBase SequenceBinding SitesDNA-Binding ProteinsElectrophoretic Mobility Shift AssayEnzyme AssaysEscherichia coli ProteinsFluorometryNucleosomesProtein BindingProtein EngineeringProtein Structure, TertiaryRecombinant Fusion ProteinsAdenosine TriphosphateAraC protein, E coliAraC Transcription FactorCHD1 protein, S cerevisiaeDNA-Binding ProteinsEscherichia coli ProteinsNucleosomesRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21969605
PMCPMC3232923
OpenAlexW2131838202

What OpenQuestion holds

Textmetadata
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.