Evidence map›Paper›PMID 22088982›Full record

ArticleDNA repair2012

Electron microscopy visualization of DNA-protein complexes formed by Ku and DNA ligase IV.

Patricia Grob, Teri T Zhang, Ryan Hannah, Hui Yang, Melissa L Hefferin, Alan E Tomkinson, Eva Nogales

Abstract read
In one paragraph

Article in DNA repair, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Consider the workhorse: Nonhomologous end-joining in budding yeast.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

7 authors.

Patricia GrobHoward Hughes Medical Institute, UC Berkeley, CA 94720-3220, United States.
Teri T Zhang
Ryan Hannah
Hui Yang
Melissa L Hefferin
Alan E Tomkinson
Eva Nogales

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
CELLULAR FUNCTIONS OF EUKARYOTIC LIGASESR01GM047251 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI DAVIS, ANTHONY J, TOMKINSON, ALAN E · 1998 to 2021
$4.7M
CELLULAR FUNCTIONS OF EUKARYOTIC DNA LIGASESR29GM047251 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI TOMKINSON, ALAN E · 1993 to 1997
–
Howard Hughes Medical InstituteNCI NIH HHS CA92584NCI NIH HHS P01 CA092584NIGMS NIH HHS GM47251NIGMS NIH HHS R01 GM047251
6 · The paper itself

Abstract

The repair of DNA double-stranded breaks (DSBs) is essential for cell viability and genome stability. Aberrant repair of DSBs has been linked with cancer predisposition and aging. During the repair of DSBs by non-homologous end joining (NHEJ), DNA ends are brought together, processed and then joined. In eukaryotes, this repair pathway is initiated by the binding of the ring-shaped Ku heterodimer and completed by DNA ligase IV. The DNA ligase IV complex, DNA ligase IV/XRRC4 in humans and Dnl4/Lif1 in yeast, is recruited to DNA ends in vitro and in vivo by an interaction with Ku and, in yeast, Dnl4/Lif1 stabilizes the binding of yKu to in vivo DSBs. Here we have analyzed the interactions of these functionally conserved eukaryotic NHEJ factors with DNA by electron microscopy. As expected, the ring-shaped Ku complex bound stably and specifically to DNA ends at physiological salt concentrations. At a ratio of 1 Ku molecule per DNA end, the majority of DNA ends were occupied by a single Ku complex with no significant formation of linear DNA multimers or circular loops. Both Dnl4/Lif1 and DNA ligase IV/XRCC4 formed complexes with Ku-bound DNA ends, resulting in intra- and intermolecular DNA end bridging, even with non-ligatable DNA ends. Together, these studies, which provide the first visualization of the conserved complex formed by Ku and DNA ligase IV at juxtaposed DNA ends by electron microscopy, suggest that the DNA ligase IV complex mediates end-bridging by engaging two Ku-bound DNA ends.

Indexed as

Antigens, NuclearBase SequenceDNA-Binding ProteinsDNA Ligase ATPDNA LigasesDNA RepairKu AutoantigenMicroscopy, ElectronModels, BiologicalMolecular Sequence DataOligonucleotidesSaccharomyces cerevisiaeStaining and LabelingSubstrate SpecificityAntigens, NuclearDNA-Binding ProteinsDNA Ligase ATPDNA LigasesDNL4 protein, S cerevisiaeKu AutoantigenLIG4 protein, humanOligonucleotidesXrcc6 protein, human

Identifiers

PMID22088982
PMCPMC3253911

What OpenQuestion holds

Textmetadata
LicenceTDM
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.