Evidence map›Paper›PMID 28414321›Full record

ArticleNature structural & molecular biology2017

An orthogonal single-molecule experiment reveals multiple-attempt dynamics of type IA topoisomerases.

Kathryn H Gunn, John F Marko, Alfonso Mondragón

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2017. 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
1.5field-weighted citation impact, top 18% 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, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. 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
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Mechanism of Type IA Topoisomerases.Molecules (Basel, Switzerland) · 2020
    Review
  13. Direct observation of helicase-topoisomerase coupling within reverse gyrase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Direct observation of topoisomerase IA gate dynamics.Nature structural & molecular biology · 2018
    Article
  15. Article
  16. Article
  17. Single-Molecule Magnetic Tweezer Analysis of Topoisomerases.Methods in molecular biology (Clifton, N.J.) · 2018
    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

3 authors at 1 institution in 1 country.

Kathryn H GunnDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.
John F MarkoDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.
Alfonso MondragónDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.ORCID http://orcid.org/0000-0002-0423-6323
Northwestern University · US

Funding

Center for 3D Structure and Physics of the GenomeU54DK107980 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI DEKKER, JOB, MIRNY, LEONID A · 2015 to 2019
$14.9M
Spatio-Temporal Organization of Chromatin and Information Transfer in CancerU54CA193419 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI O'HALLORAN, THOMAS V · 2015 to 2020
$10.4M
Structural and biophysical studies of proteins, nucleic acids, and their complexesR35GM118108 · NIGMS · NORTHWESTERN UNIVERSITY · PI Alfonso Mondragon · 2017 to 2026
$5.4M
Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
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 U54 CA193419NIDDK NIH HHS U54 DK107980NIGMS NIH HHS R01 GM051350NIGMS NIH HHS R01 GM105847NIGMS NIH HHS R35 GM118108NIGMS NIH HHS T32 GM008382
6 · The paper itself

Abstract

Topoisomerases are enzymes that are involved in maintaining the topological state of cellular DNA. Their dynamic characteristics remain poorly understood despite numerous structural, biophysical and biochemical studies. Recent single-molecule experiments revealed that an important feature of the type IA topoisomerase mechanism is the presence of pauses between relaxation events. However, these experiments could not determine whether the protein remains DNA bound during the pauses or what relationship may exist between protein domain movements and topological changes in the DNA. By combining two orthogonal single-molecule techniques, we found that E. coli topoisomerase I constantly changes conformation when attempting to modify the topology of DNA, but succeeds in only a fraction of the attempts. Thus, its mechanism can be described as a series of DNA strand-passage attempts that culminate in a successful relaxation event.

Indexed as

DNADNA Topoisomerases, Type IEscherichia coliModels, BiologicalModels, MolecularNucleic Acid ConformationProtein ConformationDNADNA Topoisomerases, Type I

Identifiers

PMID28414321
PMCPMC5516274
OpenAlexW2606937781

What OpenQuestion holds

Textmetadata
LicenceTDM
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.