Evidence map›Paper›PMID 18694512›Full record

ArticleBMC molecular biology2008

Mutational analysis of highly conserved aspartate residues essential to the catalytic core of the piggyBac transposase.

James H Keith, Cheryl A Schaeper, Tresa S Fraser, Malcolm J Fraser

Open access · bronzeAbstract read
In one paragraph

Article in BMC molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Biology · 2023
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  3. Evolution ofInsects · 2023
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  4. Article
  5. Functional Characterization of the N-Terminal Disordered Region of theInternational journal of molecular sciences · 2022
    Article
  6. Functional characterization ofJournal of Zhejiang University. Science. B · 2022
    Article
  7. Review
  8. In VivoInternational journal of molecular sciences · 2019
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. piggyBac-mediated phenotypic correction of factor VIII deficiency.Molecular therapy. Methods & clinical development · 2014
    Article
  18. Article
  19. Article
  20. piggyBac transposase tools for genome engineering.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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 1 institution in 1 country.

James H KeithUniversity of Notre Dame, Notre Dame, Indiana, USA. jkeith2@nd.edu
Cheryl A Schaeper
Tresa S Fraser
Malcolm J Fraser
University of Notre Dame · US

Funding

Transgenic engineering of Aedine mosquitoesR01AI048561 · NIAID · UNIVERSITY OF NOTRE DAME · PI FRASER, MALCOLM J. · 2001 to 2005
$1.8M
NIAID NIH HHS R01 AI048561NIAID NIH HHS R01 AI48561
6 · The paper itself

Abstract

backgroundThe piggyBac mobile element is quickly gaining popularity as a tool for the transgenesis of many eukaryotic organisms. By studying the transposase which catalyzes the movement of piggyBac, we may be able to modify this vector system to make it a more effective transgenesis tool. In a previous publication, Sarkar A, Sim C, Hong YS, Hogan JR, Fraser MJ, Robertson HM, and Collins FH have proposed the presence of the widespread 'DDE/DDD' motif for piggyBac at amino acid positions D268, D346, and D447.

resultsThis study utilizes directed mutagenesis and plasmid-based mobility assays to assess the importance of these residues as the catalytic core of the piggyBac transposase. We have functionally analyzed individual point-mutations with respect to charge and physical size in all three proposed residues of the 'DDD' motif as well as another nearby, highly conserved aspartate at D450. All of our mutations had a significant effect on excision frequency in S2 cell cultures. We have also aligned the piggyBac transposase to other close family members, both functional and non-functional, in an attempt to identify the most highly conserved regions and position a number of interesting features.

conclusionWe found all the designated DDD aspartates reside in clusters of amino acids that conserved among piggyBac family transposase members. Our results indicate that all four aspartates are necessary, to one degree or another, for excision to occur in a cellular environment, but D450 seems to have a tolerance for a glutamate substitution. All mutants tested significantly decreased excision frequency in cell cultures when compared with the wild-type transposase.

Indexed as

Amino Acid SubstitutionAspartic AcidConserved SequenceAnimalsCatalytic DomainDNA Transposable ElementsDrosophila melanogasterMothsMutagenesis, Site-DirectedSequence AlignmentTransfectionTransposasesAspartic AcidDNA Transposable ElementsTransposases

Identifiers

PMID18694512
PMCPMC2533014
OpenAlexW2110192935

What OpenQuestion holds

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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.