Evidence map›Paper›PMID 20026581›Full record

ArticleNucleic acids research2010

The multi-domain protein Np95 connects DNA methylation and histone modification.

Andrea Rottach, Carina Frauer, Garwin Pichler, Ian Marc Bonapace, Fabio Spada, Heinrich Leonhardt

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

101 citing papers in PubMed, 157 citations in OpenAlex.

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  3. UHRF1 Controls the Timing of RAD51 Removal During DNA Damage Repair Through Suppressing RFWD3.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  14. The RNA m5C Methylase NSUN2 Modulates Corneal Epithelial Wound Healing.Investigative ophthalmology & visual science · 2023
    Article
  15. Article
  16. Mechanisms of chromatin-based epigenetic inheritance.Science China. Life sciences · 2022
    Review
  17. Article
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  19. Article
  20. Genetic Studies on Mammalian DNA Methyltransferases.Advances in experimental medicine and biology · 2022
    Article

41 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 3 institutions in 2 countries.

Andrea RottachLudwig Maximilians University Munich, Department of Biology II and Center for Integrated Protein Science Munich, Grosshaderner Str. 2, 82152 Planegg-Martinsried, Germany.
Carina Frauer
Garwin Pichler
Ian Marc Bonapace
Fabio Spada
Heinrich Leonhardt
Center for Integrated Protein Science Munich · DELudwig-Maximilians-Universität München · DEUniversity of Insubria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA methylation and histone modifications play a central role in the epigenetic regulation of gene expression and cell differentiation. Recently, Np95 (also known as UHRF1 or ICBP90) has been found to interact with Dnmt1 and to bind hemimethylated DNA, indicating together with genetic studies a central role in the maintenance of DNA methylation. Using in vitro binding assays we observed a weak preference of Np95 and its SRA (SET- and Ring-associated) domain for hemimethylated CpG sites. However, the binding kinetics of Np95 in living cells was not affected by the complete loss of genomic methylation. Investigating further links with heterochromatin, we could show that Np95 preferentially binds histone H3 N-terminal tails with trimethylated (H3K9me3) but not acetylated lysine 9 via a tandem Tudor domain. This domain contains three highly conserved aromatic amino acids that form an aromatic cage similar to the one binding H3K9me3 in the chromodomain of HP1ss. Mutations targeting the aromatic cage of the Np95 tandem Tudor domain (Y188A and Y191A) abolished specific H3 histone tail binding. These multiple interactions of the multi-domain protein Np95 with hemimethylated DNA and repressive histone marks as well as with DNA and histone methyltransferases integrate the two major epigenetic silencing pathways.

Indexed as

DNA MethylationAmino Acid SequenceCCAAT-Enhancer-Binding ProteinsCell LineDNAHistonesHumansKineticsMolecular Sequence DataProtein Structure, TertiaryUbiquitin-Protein LigasesCCAAT-Enhancer-Binding ProteinsDNAHistonesUbiquitin-Protein LigasesUHRF1 protein, human

Identifiers

PMID20026581
PMCPMC2847221
OpenAlexW2039056262

What OpenQuestion holds

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LicenceCC BY-NC
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.