Evidence map›Paper›PMID 18042458›Full record

ArticleMolecular cell2007

Sae2 is an endonuclease that processes hairpin DNA cooperatively with the Mre11/Rad50/Xrs2 complex.

Bettina M Lengsfeld, Alison J Rattray, Venugopal Bhaskara, Rodolfo Ghirlando, Tanya T Paull

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 183 papers.

0numbers the graph read from it
0cells of the map it votes in
183citing papers in PubMed
13.5field-weighted citation impact, top 1% 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

183 citing papers in PubMed, 277 citations in OpenAlex.

  1. Review
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  6. eLife · 2024
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  8. Review
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  10. Review
  11. DNA damage-induced phosphorylation of CtIP at a conserved ATM/ATR site T855 promotes lymphomagenesis in mice.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Review
  13. Human RecQ Helicases in DNA Double-Strand Break Repair.Frontiers in cell and developmental biology · 2021
    Review
  14. Article
  15. CtIP promotes the motor activity of DNA2 to accelerate long-range DNA end resection.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

123 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Bettina M LengsfeldDepartment of Molecular Genetics and Microbiology, University of Texas at Austin, Austin, TX 78712, USA.
Alison J Rattray
Venugopal Bhaskara
Rodolfo Ghirlando
Tanya T Paull
The University of Texas at Austin · USFrederick National Laboratory for Cancer Research · USNational Institutes of Health · US

Funding

Mrell/Rad50/Nbs1 and DNA double strand break repairR01CA094008 · NCI · UNIVERSITY OF TEXAS AUSTIN · PI PAULL, TANYA T · 2002 to 2011
$2.8M
Intramural NIH HHSNCI NIH HHS R01 CA094008
6 · The paper itself

Abstract

Mre11/Rad50 complexes in all organisms function in the repair of DNA double-strand breaks. In budding yeast, genetic evidence suggests that the Sae2 protein is essential for the processing of hairpin DNA intermediates and meiotic double-strand breaks by Mre11/Rad50 complexes, but the biochemical basis of this functional relationship is not known. Here we demonstrate that recombinant Sae2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. Hairpin structures are not processed at the tip by Sae2 but rather at single-stranded DNA regions adjacent to the hairpin. Truncation and missense mutants of Sae2 inactivate this endonuclease activity in vitro and fail to complement Deltasae2 strains in vivo for meiosis and recombination involving hairpin intermediates, suggesting that the catalytic activities of Sae2 are important for its biological functions.

Indexed as

Nucleic Acid ConformationDNA-Binding ProteinsDNA, FungalDNA, Single-StrandedEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesMutant ProteinsPhenotypeProtein BindingRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsDNA, FungalDNA, Single-StrandedEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesMRE11 protein, S cerevisiaeMutant ProteinsRAD50 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae ProteinsSAE2 protein, S cerevisiaeXRS2 protein, S cerevisiae

Identifiers

PMID18042458
PMCPMC2194599
OpenAlexW2019239618

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.