Evidence map›Paper›PMID 16849422›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Topoisomerase IIIalpha and Bloom's helicase can resolve a mobile double Holliday junction substrate through convergent branch migration.

Jody L Plank, Jianhong Wu, Tao-Shih Hsieh

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

99 citing papers in PubMed, 154 citations in OpenAlex.

  1. Mechanisms That Govern Recombinase Fidelity Control During Eukaryotic Homologous Recombination.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    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. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Generation of double Holliday junction DNAs and their dissolution/resolution within a chromatin context.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Meiotic Crossover Patterning.Frontiers in cell and developmental biology · 2021
    Review
  16. Article
  17. Article
  18. The many lives of type IA topoisomerases.The Journal of biological chemistry · 2020
    Review
  19. Review
  20. Review

39 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Jody L PlankDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Jianhong Wu
Tao-Shih Hsieh
Duke Medical Center · USHarvard University Press · US

Funding

FUNCTION AND MECHANISM OF DNA TOPOISOMERASER01GM029006 · NIGMS · DUKE UNIVERSITY · PI HSIEH, TAO-SHIH · 1985 to 2010
$5.5M
NIGMS NIH HHS GM29006NIGMS NIH HHS R01 GM029006
6 · The paper itself

Abstract

It has long been suspected that a double Holliday junction (dHJ) could be resolved by a topoisomerase partnered with a helicase by convergent branch migration of the HJs. Genetic analysis of yeast TOP3 and SGS1 has lent considerable evidence to the notion that the protein products of these genes are involved in just such a process, although biochemical analysis of the metabolism of a dHJ has been hindered by the lack of a substrate that adequately replicates the endogenous structure. We have synthesized a dHJ substrate that recapitulates many of the features of an endogenous dHJ and represents a much earlier intermediate in the resolution pathway. Here, we show that Drosophila topoisomerase IIIalpha (Topo IIIalpha) and Blm (a homolog of Sgs1) are capable of resolving this substrate to non-cross-over products and that this activity is stimulated by replication protein A (RPA). We investigated the ability of other Drosophila topoisomerases to perform this reaction in concert with Blm and RPA and discovered that this resolution activity is unique to Topo IIIalpha. Examination of the mechanism of resolution reveals that Topo IIIalpha, Blm, and RPA resolve this substrate by convergent migration of the two HJs toward each other, collapsing the dHJ. This mechanism stands in contrast to classic resolvase activities that use a structure-specific endonuclease to cleave the HJs.

Indexed as

AnimalsCrossing Over, GeneticCross-Linking ReagentsDNA, CruciformDNA HelicasesDNA RepairDNA Topoisomerases, Type IDrosophila melanogasterDrosophila ProteinsEndonucleasesModels, BiologicalModels, GeneticRecombination, GeneticReplication Protein Ablm protein, DrosophilaCross-Linking ReagentsDNA, CruciformDNA HelicasesDNA Topoisomerases, Type IDrosophila ProteinsEndonucleasesReplication Protein A

Identifiers

PMID16849422
PMCPMC1544052
OpenAlexW2160793656

What OpenQuestion holds

Textmetadata
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.