Evidence map›Paper›PMID 17190600›Full record

ArticleCell2006

Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair.

Maria Victoria Botuyan, Joseph Lee, Irene M Ward, Ja-Eun Kim, James R Thompson, Junjie Chen, Georges Mer

Abstract read
In one paragraph

Article in Cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 577 papers.

0numbers the graph read from it
0cells of the map it votes in
577citing 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

577 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

517 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

7 authors.

Maria Victoria BotuyanDepartment of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905, USA.
Joseph Lee
Irene M Ward
Ja-Eun Kim
James R Thompson
Junjie Chen
Georges Mer

Funding

Analysis of 53BP1 function in DNA Damage-signaled pathway and TumorigenesisR01CA100109 · NCI · YALE UNIVERSITY · PI CHEN, JUNJIE · 2003 to 2010
$2.4M
Structural Basis of Cell Signaling by BRCT DomainsR01CA109449 · NCI · MAYO CLINIC ROCHESTER · PI MER, GEORGES · 2004 to 2008
$1.3M
NCI NIH HHS CA100109NCI NIH HHS R01 CA100109NCI NIH HHS R01 CA109449
6 · The paper itself

Abstract

Histone lysine methylation has been linked to the recruitment of mammalian DNA repair factor 53BP1 and putative fission yeast homolog Crb2 to DNA double-strand breaks (DSBs), but how histone recognition is achieved has not been established. Here we demonstrate that this link occurs through direct binding of 53BP1 and Crb2 to histone H4. Using X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, we show that, despite low amino acid sequence conservation, both 53BP1 and Crb2 contain tandem tudor domains that interact with histone H4 specifically dimethylated at Lys20 (H4-K20me2). The structure of 53BP1/H4-K20me2 complex uncovers a unique five-residue 53BP1 binding cage, remarkably conserved in the structure of Crb2, that best accommodates a dimethyllysine but excludes a trimethyllysine, thus explaining the methylation state-specific recognition of H4-K20. This study reveals an evolutionarily conserved molecular mechanism of targeting DNA repair proteins to DSBs by direct recognition of H4-K20me2.

Indexed as

DNA RepairAmino Acid SequenceBinding SitesCarrier ProteinsChromatinConserved SequenceCrystallography, X-RayDNA Breaks, Double-StrandedHistonesHumansIntracellular Signaling Peptides and ProteinsLysineMagnetic Resonance SpectroscopyMembrane ProteinsMethylationMolecular Sequence DataCarrier ProteinsChromatinCRB2 protein, humanHistonesIntracellular Signaling Peptides and ProteinsLysineMembrane ProteinsPhosphoproteinsTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1

Identifiers

PMID17190600
PMCPMC1804291

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.