Evidence map›Paper›PMID 22067446›Full record

ArticleNucleic acids research2012

Specialization of an Exonuclease III family enzyme in the repair of 3' DNA lesions during base excision repair in the human pathogen Neisseria meningitidis.

Jan Silhan, Krzysztofa Nagorska, Qiyuan Zhao, Kirsten Jensen, Paul S Freemont, Christoph M Tang, Geoff S Baldwin

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. DNA uptake sequences inMicrobial genomics · 2016
    Article
  5. Article
  6. Article
  7. Review
  8. Structural basis for the recognition and cleavage of abasic DNA in Neisseria meningitidis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  9. 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

7 authors at 1 institution in 1 country.

Jan SilhanDivision of Molecular Biosciences, Imperial College London, South Kensington Campus, London, SW7 2AZ, UK.
Krzysztofa Nagorska
Qiyuan Zhao
Kirsten Jensen
Paul S Freemont
Christoph M Tang
Geoff S Baldwin
Imperial College London · GB

Funding

Medical Research Council G0900888Wellcome Trust 084369/Z/07/Z
6 · The paper itself

Abstract

We have previously demonstrated that the two Exonuclease III (Xth) family members present within the obligate human pathogen Neisseria meningitidis, NApe and NExo, are important for survival under conditions of oxidative stress. Of these, only NApe possesses AP endonuclease activity, while the primary function of NExo remained unclear. We now reveal further functional specialization at the level of 3'-PO(4) processing for NExo. We demonstrate that the bi-functional meningococcal glycosylases Nth and MutM can perform strand incisions at abasic sites in addition to NApe. However, no such functional redundancy exists for the 3'-phosphatase activity of NExo, and the cytotoxicity of 3'-blocking lesions is reflected in the marked sensitivity of a mutant lacking NExo to oxidative stress, compared to strains deficient in other base excision repair enzymes. A histidine residue within NExo that is responsible for its lack of AP endonuclease activity is also important for its 3'-phosphatase activity, demonstrating an evolutionary trade off in enzyme function at the single amino acid level. This specialization of two Xth enzymes for the 3'-end processing and strand-incision reactions has not previously been observed and provides a new paradigm within the prokaryotic world for separation of these critical functions during base excision repair.

Indexed as

DNA RepairDNA DamageExodeoxyribonucleasesHistidineMicrobial ViabilityNeisseria meningitidisOxidative StressPhosphoric Monoester HydrolasesSubstrate Specificityexodeoxyribonuclease IIIExodeoxyribonucleasesHistidinePhosphoric Monoester Hydrolases

Identifiers

PMID22067446
PMCPMC3300015
OpenAlexW2052696153

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.