Evidence map›Paper›PMID 19884492›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Direct observation of twisting steps during Rad51 polymerization on DNA.

Hideyuki Arata, Aurélie Dupont, Judith Miné-Hattab, Ludovic Disseau, Axelle Renodon-Cornière, Masayuki Takahashi, Jean-Louis Viovy, Giovanni Cappello

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Visualization and quantification of nascent RAD51 filament formation at single-monomer resolution.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Recent developments in single-molecule DNA mechanics.Current opinion in structural biology · 2012
    Review
  10. Review
  11. Article
  12. Article
  13. Stepwise translocation of nucleic acid motors.Current opinion in structural biology · 2010
    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

8 authors at 3 institutions in 2 countries.

Hideyuki ArataInstitut Curie, Centre National de la Recherche Scientifique, Université Pierre et Marie Curie, Unité Mixte de Recherche 168, 75231 Paris, France.
Aurélie Dupont
Judith Miné-Hattab
Ludovic Disseau
Axelle Renodon-Cornière
Masayuki Takahashi
Jean-Louis Viovy
Giovanni Cappello
Sorbonne Université · FRCentre National de la Recherche Scientifique · FRJapan Society for the Promotion of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human recombinase hRad51 is a key protein for the maintenance of genome integrity and for cancer development. Polymerization and depolymerization of hRad51 on duplex DNA were studied here using a new generation of magnetic tweezers, measuring DNA twist in real time with a resolution of 5 degrees . Our results combined with earlier structural information suggest that DNA is somewhat less extended by hRad51 than by RecA (4.5 vs. 5.1 A per base pair) and untwisted by 18.2 degrees per base pair. They also confirm a stoichiometry of 3-4 bp per protein in the hRad51-dsDNA nucleoprotein filament. At odds with earlier claims, we show that after initial deposition of a multimeric nucleus, nucleoprotein filament growth occurs by addition/release of single proteins, involving DNA twisting steps of 65 degrees +/- 5 degrees. Simple numeric simulations show that this mechanism is an efficient way to minimize nucleoprotein filament defects. Nucleoprotein filament growth from a preformed nucleus was observed at hRad51 concentrations down to 10 nM, whereas nucleation was never observed below 100 nM in the same buffer. This behavior can be associated with the different stoichiometries of nucleation and growth. It may be instrumental in vivo to permit efficient continuation of strand exchange by hRad51 alone while requiring additional proteins such as Rad52 for its initiation, thus keeping the latter under the strict control of regulatory pathways.

Indexed as

DNAHumansMagneticsNucleic Acid ConformationNucleoproteinsPolymersRad51 RecombinaseDNANucleoproteinsPolymersRAD51 protein, humanRad51 Recombinase

Identifiers

PMID19884492
PMCPMC2780809
OpenAlexW2045177980

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.