Evidence map›Paper›PMID 29595473›Full record

ArticleeLife2018

Topoisomerase VI senses and exploits both DNA crossings and bends to facilitate strand passage.

Timothy J Wendorff, James M Berger

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

24 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Dimerization of thebioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Cryo-EM structures of the Spo11 core complex bound to DNA.Nature structural & molecular biology · 2025
    Article
  7. Review
  8. Reconstitution of SPO11-dependent double-strand break formation.bioRxiv : the preprint server for biology · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Cryo-EM structure of the Spo11 core complex bound to DNA.bioRxiv : the preprint server for biology · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. DNA topoisomerases: Advances in understanding of cellular roles and multi-protein complexes via structure-function analysis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021
    Review
  20. Mechanism and Control of Meiotic DNA Double-Strand Break Formation inFrontiers in cell and developmental biology · 2021
    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

2 authors at 2 institutions in 1 country.

Timothy J WendorffBiophysics Graduate Program, University of California, Berkeley, Berkeley, United States.
James M BergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, United States.ORCID 0000-0003-0666-1240
Johns Hopkins University · USUniversity of California, Berkeley · US

Funding

Structural and Biochemical Analyses of Type II DNA TopoisomerasesR01CA077373 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M. · 1999 to 2021
$7.6M
NCI NIH HHS R01 CA077373NIH HHS RO1 CA077373
6 · The paper itself

Abstract

Type II topoisomerases manage DNA supercoiling and aid chromosome segregation using a complex, ATP-dependent duplex strand passage mechanism. Type IIB topoisomerases and their homologs support both archaeal/plant viability and meiotic recombination. Topo VI, a prototypical type IIB topoisomerase, comprises two Top6A and two Top6B protomers; how these subunits cooperate to engage two DNA segments and link ATP turnover to DNA transport is poorly understood. Using multiple biochemical approaches, we show that Top6B, which harbors the ATPase activity of topo VI, recognizes and exploits the DNA crossings present in supercoiled DNA to stimulate subunit dimerization by ATP. Top6B self-association in turn induces extensive DNA bending, which is needed to support duplex cleavage by Top6A. Our observations explain how topo VI tightly coordinates DNA crossover recognition and ATP binding with strand scission, providing useful insights into the operation of type IIB topoisomerases and related meiotic recombination and GHKL ATPase machineries.

Indexed as

Nucleic Acid ConformationAdenosine TriphosphateArchaeal ProteinsDNA CleavageDNA, SuperhelicalDNA Topoisomerases, Type IIMethanosarcinaProtein SubunitsAdenosine TriphosphateArchaeal ProteinsDNA, SuperhelicalDNA Topoisomerases, Type IIDNA topoisomerase VIProtein SubunitsATP-dependent molecular machinesbiochemistrychemical biologyDNA topologymolecular biophysicsprotein allosteryprotein-nucleic acid interactionsstructural biologytype II topoisomerases

Identifiers

PMID29595473
PMCPMC5922973
OpenAlexW2795094088

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.