Evidence map›Paper›PMID 12242235›Full record

ArticleGenetics2002

Identification and analysis of a hyperactive mutant form of Drosophila P-element transposase.

Eileen L Beall, Matthew B Mahoney, Donald C Rio

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Maize Transposable ElementsG3 (Bethesda, Md.) · 2018
    Article
  6. Genetic and Transgenic Reagents forG3 (Bethesda, Md.) · 2017
    Article
  7. Article
  8. DNA Transposition at Work.Chemical reviews · 2016
    Review
  9. Article
  10. Article
  11. IPB7 transposase behavior in Drosophila melanogaster and Aedes aegypti.Insect biochemistry and molecular biology · 2013
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. DNA damage and L1 retrotransposition.Journal of biomedicine & biotechnology · 2006
    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

3 authors at 1 institution in 1 country.

Eileen L BeallDepartment of Molecular and Cell Biology, University of California, Berkeley, California 94720-3204, USA.
Matthew B Mahoney
Donald C Rio
University of California, Berkeley · US

Funding

MECHANISMS &REGULATION OF DROSOPHILA P ELMNT TRANSPSTNR01GM048862 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI RIO, DONALD C · 1992 to 2003
$1.4M
NIGMS NIH HHS R01GM48862
6 · The paper itself

Abstract

Transposition in many organisms is regulated to control the frequency of DNA damage caused by the DNA breakage and joining reactions. However, genetic studies in prokaryotic systems have led to the isolation of mutant transposase proteins with higher or novel activities compared to those of the wild-type protein. In the course of our study of the effects of mutating potential ATM-family DNA damage checkpoint protein kinase sites in the Drosophila P-element transposase protein, we found one mutation, S129A, that resulted in an elevated level of transposase activity using in vivo recombination assays, including P-element-mediated germline transformation. In vitro assays for P-element transposase activity indicate that the S129A mutant exhibits elevated donor DNA cleavage activity when compared to the wild-type protein, whereas the strand-transfer activity is similar to that of wild type. This difference may reflect the nature of the in vitro assays and that normally in vivo the two reactions may proceed in concert. The P-element transposase protein contains 10 potential consensus phosphorylation sites for the ATM family of PI(3)-related protein kinases. Of these 10 sites, 8 affect transposase activity either positively or negatively when substituted individually with alanine and tested in vivo. A mutant transposase protein that contains all eight N-terminal serine and threonine residues substituted with alanine is inactive and can be restored to full activity by substitution of wild-type amino acids back at only 3 of the 8 positions. These data suggest that the activity of P-element transposase may be regulated by phosphorylation and demonstrate that one mutation, S129A, results in hyperactive transposition.

Indexed as

Amino Acid SequenceAnimalsDrosophilaGerm CellsMicroinjectionsMolecular Sequence DataMutagenesisPhosphorylationTransposasesTransposases

Identifiers

PMID12242235
PMCPMC1462248
OpenAlexW2136120616

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.