Evidence map›Paper›PMID 19000038›Full record

ArticleThe Biochemical journal2009

Active site substitutions delineate distinct classes of eubacterial flap endonuclease.

Lee M Allen, Michael R G Hodskinson, Jon R Sayers

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

18 citing papers in PubMed, 20 citations in OpenAlex.

  1. DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
  2. DnaE uses strand displacement synthesis during Okazaki fragment repair.bioRxiv : the preprint server for biology · 2026
    Article
  3. Biomolecular NMR assignments · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Direct observation of DNA threading in flap endonuclease complexes.Nature structural & molecular biology · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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

3 authors at 1 institution in 1 country.

Lee M AllenThe University of Sheffield School of Medicine and Biomedical Sciences, Henry Wellcome Laboratories for Medical Research, Department of Infection and Immunity, Sheffield S102RX, UK.
Michael R G Hodskinson
Jon R Sayers
University of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council 02B1B08371Biotechnology and Biological Sciences Research Council 99B1B05418Biotechnology and Biological Sciences Research Council B19466
6 · The paper itself

Abstract

FENs (flap endonucleases) play essential roles in DNA replication, pivotally in the resolution of Okazaki fragments. In eubacteria, DNA PolI (polymerase I) contains a flap processing domain, the N-terminal 5'-->3' exonuclease. We present evidence of paralogous FEN-encoding genes present in many eubacteria. Two distinct classes of these independent FEN-encoding genes exist with four groups of eubacteria, being identified based on the number and type of FEN gene encoded. The respective proteins possess distinct motifs hallmarking their differentiation. Crucially, based on primary sequence and predicted secondary structural motifs, we reveal key differences at their active sites. These results are supported by biochemical characterization of two family members--ExoIX (exonuclease IX) from Escherichia coli and SaFEN (Staphylococcus aureus FEN). These proteins displayed marked differences in their ability to process a range of branched and linear DNA structures. On bifurcated substrates, SaFEN exhibited similar substrate specificity to previously characterized FENs. In quantitative exonuclease assays, SaFEN maintained a comparable activity with that reported for PolI. However, ExoIX showed no observable enzymatic activity. A threaded model is presented for SaFEN, demonstrating the probable interaction of this newly identified class of FEN with divalent metal ions and a branched DNA substrate. The results from the present study provide an intriguing model for the cellular role of these FEN sub-classes and illustrate the evolutionary importance of processing aberrant DNA, which has led to their maintenance alongside DNA PolI in many eubacteria.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBacteriaCatalytic DomainCloning, MolecularDNA Polymerase IEscherichia coliExodeoxyribonucleasesFlap EndonucleasesModels, BiologicalModels, MolecularMolecular Sequence DataPhosphoric Diester HydrolasesPhylogenySequence HomologyStaphylococcus aureusDNA Polymerase IExodeoxyribonucleasesexonuclease IX, E coliFlap EndonucleasesPhosphoric Diester Hydrolases

Identifiers

PMID19000038
PMCPMC2650880
OpenAlexW2072967474

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.