Evidence map›Paper›PMID 22033927›Full record

ArticleThe Journal of biological chemistry2011

Crystal structure of the chromodomain helicase DNA-binding protein 1 (Chd1) DNA-binding domain in complex with DNA.

Amit Sharma, Katherine R Jenkins, Annie Héroux, Gregory D Bowman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

30 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Biophysics of Chromatin Remodeling.Annual review of biophysics · 2021
    Review
  6. Review
  7. The Role of Non-Catalytic Domains of Hrp3 in Nucleosome Remodeling.International journal of molecular sciences · 2021
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Sequence-specific targeting of chromatin remodelers organizes precisely positioned nucleosomes throughout the genome.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017
    Review
  18. Article
  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

4 authors at 2 institutions in 1 country.

Amit SharmaThomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218.
Katherine R JenkinsThomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218.
Annie HérouxBiology Department, Brookhaven National Laboratory, Upton, New York 11973.
Gregory D BowmanThomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218. Electronic address: gdbowman@jhu.edu.
Johns Hopkins University · USBrookhaven National Laboratory · US

Funding

X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
Structural and Functional Characterization of the Chd1 Chromatin RemodelerR01GM084192 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BOWMAN, GREGORY DEAN · 2008 to 2024
$6.3M
NCRR NIH HHS P41 RR012408NIGMS NIH HHS R01 GM084192
6 · The paper itself

Abstract

Chromatin remodelers are ATP-dependent machines that dynamically alter the chromatin packaging of eukaryotic genomes by assembling, sliding, and displacing nucleosomes. The Chd1 chromatin remodeler possesses a C-terminal DNA-binding domain that is required for efficient nucleosome sliding and believed to be essential for sensing the length of DNA flanking the nucleosome core. The structure of the Chd1 DNA-binding domain was recently shown to consist of a SANT and SLIDE domain, analogous to the DNA-binding domain of the ISWI family, yet the details of how Chd1 recognized DNA were not known. Here we present the crystal structure of the Saccharomyces cerevisiae Chd1 DNA-binding domain in complex with a DNA duplex. The bound DNA duplex is straight, consistent with the preference exhibited by the Chd1 DNA-binding domain for extranucleosomal DNA. Comparison of this structure with the recently solved ISW1a DNA-binding domain bound to DNA reveals that DNA lays across each protein at a distinct angle, yet contacts similar surfaces on the SANT and SLIDE domains. In contrast to the minor groove binding seen for Isw1 and predicted for Chd1, the SLIDE domain of the Chd1 DNA-binding domain contacts the DNA major groove. The majority of direct contacts with the phosphate backbone occur only on one DNA strand, suggesting that Chd1 may not strongly discriminate between major and minor grooves.

Indexed as

ChromatinChromatin Assembly and DisassemblyCrystallography, X-RayDNADNA-Binding ProteinsDNA, FungalModels, MolecularMolecular ConformationNucleic AcidsNucleosomesProtein BindingProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCHD1 protein, S cerevisiaeChromatinDNADNA-Binding ProteinsDNA, FungalNucleic AcidsNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID22033927
PMCPMC3234930
OpenAlexW2079685157

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.