Evidence map›Paper›PMID 24352064›Full record

ArticleNature communications2013

Binding of PHF1 Tudor to H3K36me3 enhances nucleosome accessibility.

Catherine A Musselman, Matthew D Gibson, Erik W Hartwick, Justin A North, Jovylyn Gatchalian, Michael G Poirier, Tatiana G Kutateladze

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

56 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
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  3. Review
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  10. Review
  11. Guiding the HBO1 complex function through the JADE subunit.Nature structural & molecular biology · 2024
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  14. Polycomb Repressive Complex 2 in Oncology.Cancer treatment and research · 2023
    Article
  15. Histone Readers and Their Roles in Cancer.Cancer treatment and research · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

7 authors at 2 institutions in 1 country.

Catherine A Musselman1] Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA [2].
Matthew D GibsonDepartment of Physics, Ohio State University, Columbus, Ohio 43210, USA.
Erik W HartwickProgram in Structural Biology and Biochemistry, University of Colorado School of Medicine, Aurora, Colorado 80045, USA.
Justin A NorthDepartment of Physics, Ohio State University, Columbus, Ohio 43210, USA.
Jovylyn GatchalianDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA.
Michael G PoirierDepartment of Physics, Ohio State University, Columbus, Ohio 43210, USA.
Tatiana G Kutateladze1] Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado 80045, USA [2] Program in Structural Biology and Biochemistry, University of Colorado School of Medicine, Aurora, Colorado 80045, USA.
University of Colorado Denver · USThe Ohio State University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN PHARMACOLOGYT32GM007635 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI DELL'ACQUA, MARK L · 1985 to 2023
$6.1M
Mechanisms of Chromatin Transcriptional RegulationR01GM083055 · NIGMS · OHIO STATE UNIVERSITY · PI POIRIER, MICHAEL GUY · 2008 to 2016
$2.7M
Molecular analysis of methylated p53R01GM101664 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2013 to 2016
$1.7M
Molecular analysis of CHD4R01GM096863 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2011 to 2014
$1.4M
Role of Polycomblike1-histone interaction in PRC2 activitiesF31CA189487 · NCI · UNIVERSITY OF COLORADO DENVER · PI GATCHALIAN, JOVYLYN · 2014 to 2016
$70k
NCI NIH HHS F31 CA189487NIGMS NIH HHS GM083055NIGMS NIH HHS GM096863NIGMS NIH HHS GM101664NIGMS NIH HHS R01 GM083055NIGMS NIH HHS R01 GM096863NIGMS NIH HHS R01 GM101664NIGMS NIH HHS T32 GM007635
6 · The paper itself

Abstract

The Tudor domain of human PHF1 recognizes trimethylated lysine 36 of histone H3 (H3K36me3). This interaction modulates the methyltransferase activity of the PRC2 complex and has a role in retention of PHF1 at DNA damage sites. We have previously determined the structural basis for the association of Tudor with a methylated histone peptide. Here we detail the molecular mechanism of binding of the Tudor domain to the H3KC36me3-nucleosome core particle (H3KC36me3-NCP). Using a combination of TROSY NMR and FRET, we show that Tudor concomitantly interacts with H3K36me3 and DNA. Binding of the PHF1 Tudor domain to the H3KC36me3-NCP stabilizes the nucleosome in a conformation in which the nucleosomal DNA is more accessible to DNA-binding regulatory proteins. Our data provide a mechanistic explanation for the consequence of reading of the active mark H3K36me3 by the PHF1 Tudor domain.

Indexed as

DNADNA-Binding ProteinsDNA DamageFluorescence Resonance Energy TransferHistonesHumansLysineMagnetic Resonance SpectroscopyNucleosomesPeptidesPolycomb-Group ProteinsProtein BindingProtein Structure, TertiaryTranscription FactorsDNADNA-Binding ProteinsHistonesLysineNucleosomesPeptidesPHF1 protein, humanPolycomb-Group ProteinsTranscription Factors

Identifiers

PMID24352064
PMCPMC4007151
OpenAlexW2032656312

What OpenQuestion holds

Textmetadata
LicenceTDM
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.