Evidence map›Paper›PMID 20613843›Full record

ArticleNature2010

Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b.

Lei Zeng, Qiang Zhang, Side Li, Alexander N Plotnikov, Martin J Walsh, Ming-Ming Zhou

Open access · hybridAbstract read
In one paragraph

Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers.

0numbers the graph read from it
0cells of the map it votes in
174citing papers in PubMed
12.2field-weighted citation impact, top 1% 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

174 citing papers in PubMed, 308 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. TheInternational journal of molecular sciences · 2024
    Article
  9. Review
  10. Article
  11. Article
  12. Chromatin remodellers as therapeutic targets.Nature reviews. Drug discovery · 2024
    Review
  13. Article
  14. Article
  15. Review
  16. Assessing the functional roles of coevolving PHD finger residues.Protein science : a publication of the Protein Society · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

114 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

6 authors at 1 institution in 1 country.

Lei ZengDepartment of Structural and Chemical Biology, Mount Sinai School of Medicine, 1425 Madison Avenue, Box 1677, New York, New York 10029, USA.
Qiang Zhang
Side Li
Alexander N Plotnikov
Martin J Walsh
Ming-Ming Zhou
Icahn School of Medicine at Mount Sinai · US

Funding

Chemical Genomics Paradigm for Epigentic RegulationR01HG004508 · NHGRI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI ZHOU, MING-MING · 2008 to 2014
$6.7M
STRUCTURE OF PROTEIN MODULES IN CHROMATIN REMODELINGR01CA087658 · NCI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI ZHOU, MING-MING · 2000 to 2016
$4.8M
NCI NIH HHS R01 CA087658NHGRI NIH HHS R01 HG004508
6 · The paper itself

Abstract

Histone lysine acetylation and methylation have an important role during gene transcription in a chromatin context. Knowledge concerning the types of protein modules that can interact with acetyl-lysine has so far been limited to bromodomains. Recently, a tandem plant homeodomain (PHD) finger (PHD1-PHD2, or PHD12) of human DPF3b, which functions in association with the BAF chromatin remodelling complex to initiate gene transcription during heart and muscle development, was reported to bind histones H3 and H4 in an acetylation-sensitive manner, making it the first alternative to bromodomains for acetyl-lysine binding. Here we report the structural mechanism of acetylated histone binding by the double PHD fingers of DPF3b. Our three-dimensional solution structures and biochemical analysis of DPF3b highlight the molecular basis of the integrated tandem PHD finger, which acts as one functional unit in the sequence-specific recognition of lysine-14-acetylated histone H3 (H3K14ac). Whereas the interaction with H3 is promoted by acetylation at lysine 14, it is inhibited by methylation at lysine 4, and these opposing influences are important during transcriptional activation of the mouse DPF3b target genes Pitx2 and Jmjd1c. Binding of this tandem protein module to chromatin can thus be regulated by different histone modifications during the initiation of gene transcription.

Indexed as

Zinc FingersAcetylationAnimalsCell LineDNA-Binding ProteinsHistonesHumansLysineMiceModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein FoldingStructure-Activity RelationshipSubstrate SpecificityThermodynamicsTranscriptional ActivationDNA-Binding ProteinsDPF3 protein, humanHistonesLysineTranscription Factors

Identifiers

PMID20613843
PMCPMC2901902
OpenAlexW2069157717

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.