Evidence map›Paper›PMID 23262225›Full record

ArticleNucleic acids research2013

Solution conformations of early intermediates in Mos1 transposition.

Maxime G Cuypers, Maryia Trubitsyna, Philip Callow, V Trevor Forsyth, Julia M Richardson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
7.2field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structural Determinants of Sleeping Beauty Transposase Activity.Molecular therapy : the journal of the American Society of Gene Therapy · 2016
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mechanisms of DNA Transposition.Microbiology spectrum · 2015
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Target capture during Mos1 transposition.The Journal of biological chemistry · 2014
    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

5 authors at 1 institution in 2 countries.

Maxime G CuypersLife Sciences Group, Institut Laue Langevin (ILL), 6 rue Jules Horowitz, 38042 Grenoble, France.
Maryia Trubitsyna
Philip Callow
V Trevor Forsyth
Julia M Richardson
University of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust 085176/Z/08/Z
6 · The paper itself

Abstract

DNA transposases facilitate genome rearrangements by moving DNA transposons around and between genomes by a cut-and-paste mechanism. DNA transposition proceeds in an ordered series of nucleoprotein complexes that coordinate pairing and cleavage of the transposon ends and integration of the cleaved ends at a new genomic site. Transposition is initiated by transposase recognition of the inverted repeat sequences marking each transposon end. Using a combination of solution scattering and biochemical techniques, we have determined the solution conformations and stoichiometries of DNA-free Mos1 transposase and of the transposase bound to a single transposon end. We show that Mos1 transposase is an elongated homodimer in the absence of DNA and that the N-terminal 55 residues, containing the first helix-turn-helix motif, are required for dimerization. This arrangement is remarkably different from the compact, crossed architecture of the dimer in the Mos1 paired-end complex (PEC). The transposase remains elongated when bound to a single-transposon end in a pre-cleavage complex, and the DNA is bound predominantly to one transposase monomer. We propose that a conformational change in the single-end complex, involving rotation of one half of the transposase along with binding of a second transposon end, could facilitate PEC assembly.

Indexed as

DimerizationDNADNA-Binding ProteinsDNA Transposable ElementsModels, MolecularNeutron DiffractionProtein Structure, TertiaryScattering, Small AngleTransposasesX-Ray DiffractionDNADNA-Binding ProteinsDNA Transposable Elementsmariner transposasesTransposases

Identifiers

PMID23262225
PMCPMC3561948
OpenAlexW2145462330

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.