Evidence map›Paper›PMID 16107854›Full record

ArticleNature2005

Endonucleolytic processing of covalent protein-linked DNA double-strand breaks.

Matthew J Neale, Jing Pan, Scott Keeney

Abstract read
In one paragraph

Article in Nature, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 381 papers.

0numbers the graph read from it
0cells of the map it votes in
381citing papers in PubMed
–field-weighted citation impact
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

381 citing papers in PubMed.

  1. Controlling Meiotic Double-Strand Break Formation in Mice: A Web of Multivalent Protein-Protein Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. Rap1-mediated steric hindrance protects telomeres from MRX sensing.Nature structural & molecular biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. The histone variant H2A.W restricts heterochromatic crossovers inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

321 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

3 authors.

Matthew J NealeMolecular Biology Programs, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
Jing Pan
Scott Keeney

Funding

Mechanism of meiotic recombination in yeastR01GM058673 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI KEENEY, SCOTT · 1999 to 2015
$6.0M
Role of Spo11 and recombination in mouse meiosisR01HD040916 · NICHD · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI JASIN, MARIA · 2001 to 2011
$5.4M
NICHD NIH HHS R01 HD040916NIGMS NIH HHS R01 GM058673
6 · The paper itself

Abstract

DNA double-strand breaks (DSBs) with protein covalently attached to 5' strand termini are formed by Spo11 to initiate meiotic recombination. The Spo11 protein must be removed for the DSB to be repaired, but the mechanism for removal is unclear. Here we show that meiotic DSBs in budding yeast are processed by endonucleolytic cleavage that releases Spo11 attached to an oligonucleotide with a free 3'-OH. Two discrete Spo11-oligonucleotide complexes were found in equal amounts, differing with respect to the length of the bound DNA. We propose that these forms arise from different spacings of strand cleavages flanking the DSB, with every DSB processed asymmetrically. Thus, the ends of a single DSB may be biochemically distinct at or before the initial processing step-much earlier than previously thought. SPO11-oligonucleotide complexes were identified in extracts of mouse testis, indicating that this mechanism is evolutionarily conserved. Oligonucleotide-topoisomerase II complexes were also present in extracts of vegetative yeast, although not subject to the same genetic control as for generating Spo11-oligonucleotide complexes. Our findings suggest a general mechanism for repair of protein-linked DSBs.

Indexed as

DNA DamageAnimalsCell Cycle ProteinsDNADNA-Binding ProteinsDNA Topoisomerases, Type IIEndodeoxyribonucleasesEndonucleasesEsterasesExodeoxyribonucleasesMaleMeiosisMeiotic Recombination Protein SPO11MiceNuclear ProteinsPhosphate-Binding ProteinsCell Cycle ProteinsDmc1 protein, mouseDMC1 protein, S cerevisiaeDNADNA-Binding ProteinsDNA Topoisomerases, Type IIEndodeoxyribonucleasesEndonucleasesEsterasesExodeoxyribonucleasesMeiotic Recombination Protein SPO11MRE11 protein, S cerevisiaeNuclear ProteinsPhosphate-Binding ProteinsRAD50 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSAE2 protein, S cerevisiaeXRS2 protein, S cerevisiae

Identifiers

PMID16107854
PMCPMC1262668

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.