Evidence map›Paper›PMID 25232096›Full record

ArticleNucleic acids research2014

Single-molecule analysis uncovers the difference between the kinetics of DNA decatenation by bacterial topoisomerases I and III.

Ksenia Terekhova, John F Marko, Alfonso Mondragón

Abstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 citing papers in PubMed.

  1. Article
  2. Mechanistic basis for relaxation of DNA supercoils by human topoisomerase IIIα-RMI1-RMI2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
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  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Direct observation of topoisomerase IA gate dynamics.Nature structural & molecular biology · 2018
    Article
  16. Article
  17. Single-Molecule Magnetic Tweezer Analysis of Topoisomerases.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  18. Article
  19. Article
  20. 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

3 authors.

Ksenia TerekhovaDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
John F MarkoDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA Department of Physics and Astronomy, Northwestern University, Evanston, IL 60208, USA.
Alfonso MondragónDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA a-mondragon@northwestern.edu.

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WIDOM, JONATHAN · 2009 to 2013
$12.8M
STRUCTURE/FUNCTION STUDIES OF TYPE I TOPOISOMERASESR01GM051350 · NIGMS · NORTHWESTERN UNIVERSITY · PI MONDRAGON, ALFONSO · 1994 to 2017
$3.9M
Activities of nucleoprotein complexes visualized in single-molecule experimentsR01GM105847 · NIGMS · NORTHWESTERN UNIVERSITY · PI MARKO, JOHN F · 2013 to 2025
$2.5M
NCI NIH HHS 1U54CA143869NCI NIH HHS P30 CA060553NCI NIH HHS U54 CA143869NIGMS NIH HHS 1R01GM105847NIGMS NIH HHS R01 GM051350NIGMS NIH HHS R01GM51350
6 · The paper itself

Abstract

Escherichia coli topoisomerases I and III can decatenate double-stranded DNA (dsDNA) molecules containing single-stranded DNA regions or nicks as well as relax negatively supercoiled DNA. Although the proteins share a mechanism of action and have similar structures, they participate in different cellular processes. Whereas topoisomerase III is a more efficient decatenase than topoisomerase I, the opposite is true for DNA relaxation. In order to investigate the differences in the mechanism of these two prototypical type IA topoisomerases, we studied DNA decatenation at the single-molecule level using braids of intact dsDNA and nicked dsDNA with bulges. We found that neither protein decatenates an intact DNA braid. In contrast, both enzymes exhibited robust decatenation activity on DNA braids with a bulge. The experiments reveal that a main difference between the unbraiding mechanisms of these topoisomerases lies in the pauses between decatenation cycles. Shorter pauses for topoisomerase III result in a higher decatenation rate. In addition, topoisomerase III shows a strong dependence on the crossover angle of the DNA strands. These real-time observations reveal the kinetic characteristics of the decatenation mechanism and help explain the differences between their activities.

Indexed as

DNA, CatenatedDNA Topoisomerases, Type IEscherichia coliEscherichia coli ProteinsKineticsDNA, CatenatedDNA Topoisomerases, Type IEscherichia coli Proteins

Identifiers

PMID25232096
PMCPMC4191389

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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.