Evidence map›Paper›PMID 19129187›Full record

ArticleThe Journal of biological chemistry2009

An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases.

Joseph T P Yeeles, Richard Cammack, Mark S Dillingham

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

69 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. The CRISPR-associated Cas4 protein fromCurrent research in microbial sciences · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021
    Review
  14. Frontiers in microbiology · 2021
    Article
  15. Article
  16. Article
  17. UvrC Coordinates an OJournal of the American Chemical Society · 2020
    Article
  18. Article
  19. Article
  20. Article

9 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 at 2 institutions in 1 country.

Joseph T P YeelesDNA-Protein Interactions Unit, Department of Biochemistry, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom.
Richard Cammack
Mark S Dillingham
King's College London · GBUniversity of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

The bacterial helicase-nuclease complex AddAB converts double-stranded DNA breaks into substrates for RecA-dependent recombinational repair. Here we show that the AddB subunit contains a novel class of nuclease domain distinguished by the presence of an iron-sulfur cluster. The cluster is coordinated by an unusual arrangement of cysteine residues that originate from both sides of the AddB nuclease, forming an "iron staple" that is required for the local structural integrity of this domain. Disruption of the iron-sulfur cluster by mutagenesis eliminates the ability of AddAB to bind to duplex DNA ends without affecting the single-stranded DNA-dependent ATPase activity. Sequence analysis suggests that a related iron staple nuclease domain is present in the eukaryotic DNA replication/repair factor Dna2, where it is also associated with a DNA helicase motor.

Indexed as

DNA Breaks, Double-StrandedBacillus subtilisBacterial ProteinsDNA, BacterialDNA HelicasesExodeoxyribonucleasesIronProtein BindingProtein Structure, TertiarySaccharomyces cerevisiae ProteinsSequence Analysis, ProteinSequence Homology, Amino AcidSulfurAddAB enzymeBacterial ProteinsDNA2 protein, S cerevisiaeDNA, BacterialDNA HelicasesExodeoxyribonucleasesIronSaccharomyces cerevisiae ProteinsSulfur

Identifiers

PMID19129187
PMCPMC2658068
OpenAlexW2090953848

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.