Evidence map›Paper›PMID 21526145›Full record

ArticlePloS one2011

The telomere binding protein TRF2 induces chromatin compaction.

Asmaa M Baker, Qiang Fu, William Hayward, Samuel Victoria, Ilene M Pedroso, Stuart M Lindsay, Terace M Fletcher

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. TRF1 and TRF2: pioneering targets in telomere-based cancer therapy.Journal of cancer research and clinical oncology · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. The Intra- and Extra-Telomeric Role of TRF2 in the DNA Damage Response.International journal of molecular sciences · 2021
    Review
  8. Article
  9. Emerging roles of telomeric chromatin alterations in cancer.Journal of experimental & clinical cancer research : CR · 2019
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Chromatin structure in telomere dynamics.Frontiers in oncology · 2013
    Article
  18. Article
  19. 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.

Asmaa M BakerDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida, United States of America.
Qiang Fu
William Hayward
Samuel Victoria
Ilene M Pedroso
Stuart M Lindsay
Terace M Fletcher
University of Miami · USArizona State University · US

Funding

Structural Analysis of Telomere ChromatinF31GM075427 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BAKER, ASMAA M. · 2005 to 2007
$113k
NIGMS NIH HHS F31 GM075427NIGMS NIH HHS F31-GM75427-01
6 · The paper itself

Abstract

Mammalian telomeres are specialized chromatin structures that require the telomere binding protein, TRF2, for maintaining chromosome stability. In addition to its ability to modulate DNA repair activities, TRF2 also has direct effects on DNA structure and topology. Given that mammalian telomeric chromatin includes nucleosomes, we investigated the effect of this protein on chromatin structure. TRF2 bound to reconstituted telomeric nucleosomal fibers through both its basic N-terminus and its C-terminal DNA binding domain. Analytical agarose gel electrophoresis (AAGE) studies showed that TRF2 promoted the folding of nucleosomal arrays into more compact structures by neutralizing negative surface charge. A construct containing the N-terminal and TRFH domains together altered the charge and radius of nucleosomal arrays similarly to full-length TRF2 suggesting that TRF2-driven changes in global chromatin structure were largely due to these regions. However, the most compact chromatin structures were induced by the isolated basic N-terminal region, as judged by both AAGE and atomic force microscopy. Although the N-terminal region condensed nucleosomal array fibers, the TRFH domain, known to alter DNA topology, was required for stimulation of a strand invasion-like reaction with nucleosomal arrays. Optimal strand invasion also required the C-terminal DNA binding domain. Furthermore, the reaction was not stimulated on linear histone-free DNA. Our data suggest that nucleosomal chromatin has the ability to facilitate this activity of TRF2 which is thought to be involved in stabilizing looped telomere structures.

Indexed as

Chromatin Assembly and DisassemblyAnimalsChickensChromatinDNAHeLa CellsHumansMicroscopy, Atomic ForceMutant ProteinsNucleosomesProtein BindingProtein Structure, TertiaryStatic ElectricityTelomereTelomeric Repeat Binding Protein 2ChromatinDNAMutant ProteinsNucleosomesTelomeric Repeat Binding Protein 2

Identifiers

PMID21526145
PMCPMC3079743
OpenAlexW1968527827

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.