Evidence map›Paper›PMID 15340089›Full record

ArticleMolecular and cellular biology2004

Early intermediates of mariner transposition: catalysis without synapsis of the transposon ends suggests a novel architecture of the synaptic complex.

Karen Lipkow, Nicolas Buisine, David J Lampe, Ronald Chalmers

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.6field-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

21 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  9. DDE transposases: Structural similarity and diversity.Advanced drug delivery reviews · 2010
    Review
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  12. Review
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  18. Birth of a chimeric primate gene by capture of the transposase gene from a mobile element.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  19. Article
  20. Assembly of the mariner Mos1 synaptic complex.Molecular and cellular biology · 2005
    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

4 authors at 2 institutions in 2 countries.

Karen LipkowDepartment of Biochemistry, University of Oxford, United Kingdom.
Nicolas Buisine
David J Lampe
Ronald Chalmers
University of Oxford · GBDuquesne University · US

Funding

Wellcome Trust
6 · The paper itself

Abstract

The mariner family is probably the most widely distributed family of transposons in nature. Although these transposons are related to the well-studied bacterial insertion elements, there is evidence for major differences in their reaction mechanisms. We report the identification and characterization of complexes that contain the Himar1 transposase bound to a single transposon end. Titrations and mixing experiments with the native transposase and transposase fusions suggested that they contain different numbers of transposase monomers. However, the DNA protection footprints of the two most abundant single-end complexes are identical. This indicates that some transposase monomers may be bound to the transposon end solely by protein-protein interactions. This would mean that the Himar1 transposase can dimerize independently of the second transposon end and that the architecture of the synaptic complex has more in common with V(D)J recombination than with bacterial insertion elements. Like V(D)J recombination and in contrast to the case for bacterial elements, Himar1 catalysis does not appear to depend on synapsis of the transposon ends, and the single-end complexes are active for nicking and probably for cleavage. We discuss the role of this single-end activity in generating the mutations that inactivate the vast majority of mariner elements in eukaryotes.

Indexed as

AnimalsBase SequenceDNA-Binding ProteinsDNA Transposable ElementsDrosophilaDrosophila ProteinsGenes, InsectMutationRecombinant Fusion ProteinsTransposasesDNA-Binding ProteinsDNA Transposable ElementsDrosophila Proteinsmariner transposasesRecombinant Fusion ProteinsTc1 transposaseTransposases

Identifiers

PMID15340089
PMCPMC515030
OpenAlexW2154021943

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.