Evidence map›Paper›PMID 12730170›Full record

ArticleJournal of bacteriology2003

Repair system for noncanonical purines in Escherichia coli.

Nicholas E Burgis, Jason J Brucker, Richard P Cunningham

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2003. 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
5.1field-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

29 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Comment on "A commensal strain ofScience advances · 2019
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Endonuclease V: an unusual enzyme for repair of DNA deamination.Cellular and molecular life sciences : CMLS · 2013
    Review
  12. Review
  13. Article
  14. Defects in purine nucleotide metabolism lead to substantial incorporation of xanthine and hypoxanthine into DNA and RNA.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

3 authors at 2 institutions in 1 country.

Nicholas E BurgisDepartment of Biological Sciences, The University at Albany, State University of New York, Albany, New York 12222, USA.
Jason J Brucker
Richard P Cunningham
Albany State University · USUniversity at Albany, State University of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Exposure of Escherichia coli strains deficient in molybdopterin biosynthesis (moa) to the purine base N-6-hydroxylaminopurine (HAP) is mutagenic and toxic. We show that moa mutants exposed to HAP also exhibit elevated mutagenesis, a hyperrecombination phenotype, and increased SOS induction. The E. coli rdgB gene encodes a protein homologous to a deoxyribonucleotide triphosphate pyrophosphatase from Methanococcus jannaschii that shows a preference for purine base analogs. moa rdgB mutants are extremely sensitive to killing by HAP and exhibit increased mutagenesis, recombination, and SOS induction upon HAP exposure. Disruption of the endonuclease V gene, nfi, rescues the HAP sensitivity displayed by moa and moa rdgB mutants and reduces the level of recombination and SOS induction, but it increases the level of mutagenesis. Our results suggest that endonuclease V incision of DNA containing HAP leads to increased recombination and SOS induction and even cell death. Double-strand break repair mutants display an increase in HAP sensitivity, which can be reversed by an nfi mutation. This suggests that cell killing may result from an increase in double-strand breaks generated when replication forks encounter endonuclease V-nicked DNA. We propose a pathway for the removal of HAP from purine pools, from deoxynucleotide triphosphate pools, and from DNA, and we suggest a general model for excluding purine base analogs from DNA. The system for HAP removal consists of a molybdoenzyme, thought to detoxify HAP, a deoxyribonucleotide triphosphate pyrophosphatase that removes noncanonical deoxyribonucleotide triphosphates from replication precursor pools, and an endonuclease that initiates the removal of HAP from DNA.

Indexed as

CoenzymesAdenineBacterial ProteinsChromosome BreakageDeoxyribonuclease (Pyrimidine Dimer)DNADNA RepairDNA ReplicationEndodeoxyribonucleasesEscherichia coliEscherichia coli ProteinsLexA Repressor ProteinMetalloproteinsMolybdenum CofactorsMutagenesisMutagens6-N-hydroxylaminopurineAdenineBacterial ProteinsCoenzymesDeoxyribonuclease (Pyrimidine Dimer)DNAEndodeoxyribonucleasesEscherichia coli ProteinsLexA Repressor ProteinMetalloproteinsMolybdenum CofactorsmolybdopterinMutagensPteridinesPurinesPyrophosphatasesRdgB protein, E coliSerine Endopeptidases

Identifiers

PMID12730170
PMCPMC154070
OpenAlexW2103649268

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.