Evidence map›Paper›PMID 33671470›Full record

ArticleInternational journal of molecular sciences2021

G-Quadruplex Structures Colocalize with Transcription Factories and Nuclear Speckles Surrounded by Acetylated and Dimethylated Histones H3.

Denisa Komůrková, Alena Svobodová Kovaříková, Eva Bártová

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

21 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. PXL: a Nucleic Acid-Binding Module of Promyelocytic Leukemia Protein.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
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  16. Article
  17. Article
  18. Article
  19. Chromatin Hubs: A biological and computational outlook.Computational and structural biotechnology journal · 2022
    Review
  20. Review
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

3 authors at 1 institution in 1 country.

Denisa KomůrkováInstitute of Biophysics of the Czech Academy of Sciences, Department of Molecular Cytology and Cytometry, Královopolská 135, 612 65 Brno, Czech Republic.ORCID 0000-0002-2046-9610
Alena Svobodová KovaříkováInstitute of Biophysics of the Czech Academy of Sciences, Department of Molecular Cytology and Cytometry, Královopolská 135, 612 65 Brno, Czech Republic.
Eva BártováInstitute of Biophysics of the Czech Academy of Sciences, Department of Molecular Cytology and Cytometry, Královopolská 135, 612 65 Brno, Czech Republic.ORCID 0000-0003-1299-0470
Czech Academy of Sciences, Institute of Biophysics · CZ

Funding

Czech Academy of Sciences 68081707Grantová Agentura České Republiky 18-07384S
6 · The paper itself

Abstract

G-quadruplexes (G4s) are four-stranded helical structures that regulate several nuclear processes, including gene expression and telomere maintenance. We observed that G4s are located in GC-rich (euchromatin) regions and outside the fibrillarin-positive compartment of nucleoli. Genomic regions around G4s were preferentially H3K9 acetylated and H3K9 dimethylated, but H3K9me3 rarely decorated G4 structures. We additionally observed the variability in the number of G4s in selected human and mouse cell lines. We found the highest number of G4s in human embryonic stem cells. We observed the highest degree of colocalization between G4s and transcription factories, positive on the phosphorylated form of RNA polymerase II (RNAP II). Similarly, a high colocalization rate was between G4s and nuclear speckles, enriched in pre-mRNA splicing factor SC-35. PML bodies, the replication protein SMD1, and Cajal bodies colocalized with G4s to a lesser extent. Thus, G4 structures seem to appear mainly in nuclear compartments transcribed via RNAP II, and pre-mRNA is spliced via the SC-35 protein. However, α-amanitin, an inhibitor of RNAP II, did not affect colocalization between G4s and transcription factories as well as G4s and SC-35-positive domains. In addition, irradiation by γ-rays did not change a mutual link between G4s and DNA repair proteins (G4s/γH2AX, G4s/53BP1, and G4s/MDC1), accumulated into DNA damage foci. Described characteristics of G4s seem to be the manifestation of pronounced G4s stability that is likely maintained not only via a high-order organization of these structures but also by a specific histone signature, including H3K9me2, responsible for chromatin compaction.

Indexed as

G-QuadruplexesTranscription, GeneticAcetylationAnimalsBase CompositionCell LineCell NucleolusCell NucleusChromatinDNADNA RepairEpigenesis, GeneticHistonesHumansInclusion BodiesMethylationChromatinDNAHistonesDNA repairepigeneticsG-quadruplex structurenuclear bodiesnuclear specklestranscription factories

Identifiers

PMID33671470
PMCPMC7922289
OpenAlexW3132778387

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.