Evidence map›Paper›PMID 1710617›Full record

ArticleJournal of bacteriology1991

Escherichia coli Fpg protein and UvrABC endonuclease repair DNA damage induced by methylene blue plus visible light in vivo and in vitro.

H Czeczot, B Tudek, B Lambert, J Laval, S Boiteux

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 101 citations in OpenAlex.

  1. Dyes in aquaculture and reference points for action.EFSA journal. European Food Safety Authority · 2017
    Article
  2. UvrA expression ofJournal of food science and technology · 2017
    Article
  3. Review
  4. Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  5. DNA glycosylases search for and remove oxidized DNA bases.Environmental and molecular mutagenesis · 2013
    Review
  6. Article
  7. The role of Fpg protein in UVC-induced DNA lesions.Redox report : communications in free radical research · 2012
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Cancer risk and oxidative DNA damage in man.Journal of molecular medicine (Berlin, Germany) · 1996
    Review
  19. Substrate spectrum of human excinuclease: repair of abasic sites, methylated bases, mismatches, and bulky adducts.Proceedings of the National Academy of Sciences of the United States of America · 1994
    Article
  20. 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

5 authors at 1 institution in 1 country.

H CzeczotGroupe Réparation des lésions radio-chimioinduites, UA158 CNRS, U140 INSERM, Institut Gustave-Roussy, Villejuif, France.
B Tudek
B Lambert
J Laval
S Boiteux
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

pBR322 plasmid DNA was treated with methylene blue plus visible light (MB-light) and tested for transformation efficiency in Escherichia coli mutants defective in either formamidopyrimidine-DNA glycosylase (Fpg protein) and/or UvrABC endonuclease. The survival of pBR322 DNA treated with MB-light was not significantly reduced when transformed into either fpg-1 or uvrA single mutants compared with that in the wild-type strain. In contrast, the survival of MB-light-treated pBR322 DNA was greatly reduced in the fpg-1 uvrA double mutant. The synergistic effect of these two mutations was not observed in transformation experiments using pBR322 DNA treated with methyl methanesulfonate, UV light at 254 nm, or ionizing radiation. In vitro experiments showed that MB-light-treated pBR322 DNA is a substrate for the Fpg protein and UvrABC endonuclease. The number of sites sensitive to cleavage by either Fpg protein or UvrABC endonuclease was 10-fold greater than the number of apurinic-apyrimidinic sites indicated as Nfo protein (endonuclease IR)-sensitive sites. Seven Fpg protein-sensitive sites per PBR322 molecule were required to produce a lethal hit when transformed into the uvrA fpg-1 mutant. These results suggest that MB-light induces DNA base modifications which are lethal and that these modifications are repaired by Fpg protein and UvrABC endonuclease in vivo and in vitro. Therefore, one of the physiological functions of Fpg protein might be to repair DNA base damage induced by photosensitizers and light.

Indexed as

Escherichia coli ProteinsBacterial ProteinsDeoxyribonuclease IV (Phage T4-Induced)DNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA DamageDNA-Formamidopyrimidine GlycosylaseDNA RepairDose-Response Relationship, DrugEndodeoxyribonucleasesEscherichia coliGamma RaysLightMethylene BlueMethyl MethanesulfonateN-Glycosyl HydrolasesBacterial ProteinsDeoxyribonuclease IV (Phage T4-Induced)DNADNA-(Apurinic or Apyrimidinic Site) LyaseDNA-Formamidopyrimidine GlycosylaseDNA-formamidopyrimidine glycosylase, E coliEndodeoxyribonucleasesendodeoxyribonuclease uvrABCendonuclease IV, E coliEscherichia coli ProteinsMethylene BlueMethyl MethanesulfonateN-Glycosyl Hydrolases

Identifiers

PMID1710617
PMCPMC207954
OpenAlexW1921577841

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.