Evidence map›Paper›PMID 21421557›Full record

ArticleNucleic acids research2011

Direct measurement of DNA bending by type IIA topoisomerases: implications for non-equilibrium topology simplification.

Ashley H Hardin, Susanta K Sarkar, Yeonee Seol, Grace F Liou, Neil Osheroff, Keir C Neuman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Chromatinization Modulates Topoisomerase II Processivity.bioRxiv : the preprint server for biology · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. DNA-Topology Simplification by Topoisomerases.Molecules (Basel, Switzerland) · 2021
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

6 authors at 2 institutions in 1 country.

Ashley H HardinLaboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Susanta K Sarkar
Yeonee Seol
Grace F Liou
Neil Osheroff
Keir C Neuman
National Institutes of Health · USNational Heart Lung and Blood Institute · US

Funding

FUNCTION AND BIOLOGY OF EUKARYOTIC DNA TOPOISOMERASESR01GM033944 · NIGMS · VANDERBILT UNIVERSITY · PI OSHEROFF, NEIL · 1985 to 2015
$5.5M
Intramural NIH HHSNIGMS NIH HHS GM033944NIGMS NIH HHS R01 GM033944
6 · The paper itself

Abstract

Type IIA topoisomerases modify DNA topology by passing one segment of duplex DNA (transfer or T-segment) through a transient double-strand break in a second segment of DNA (gate or G-segment) in an ATP-dependent reaction. Type IIA topoisomerases decatenate, unknot and relax supercoiled DNA to levels below equilibrium, resulting in global topology simplification. The mechanism underlying this non-equilibrium topology simplification remains speculative. The bend angle model postulates that non-equilibrium topology simplification scales with the bend angle imposed on the G-segment DNA by the binding of a type IIA topoisomerase. To test this bend angle model, we used atomic force microscopy and single-molecule Förster resonance energy transfer to measure the extent of bending imposed on DNA by three type IIA topoisomerases that span the range of topology simplification activity. We found that Escherichia coli topoisomerase IV, yeast topoisomerase II and human topoisomerase IIα each bend DNA to a similar degree. These data suggest that DNA bending is not the sole determinant of non-equilibrium topology simplification. Rather, they suggest a fundamental and conserved role for DNA bending in the enzymatic cycle of type IIA topoisomerases.

Indexed as

Antigens, NeoplasmDNADNA-Binding ProteinsDNA Topoisomerases, Type IIFluorescence Resonance Energy TransferHumansMicroscopy, Atomic ForceNucleic Acid ConformationAntigens, NeoplasmDNADNA-Binding ProteinsDNA Topoisomerases, Type II

Identifiers

PMID21421557
PMCPMC3141238
OpenAlexW2103793558

What OpenQuestion holds

Textmetadata
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.