Evidence map›Paper›PMID 22417940›Full record

ArticleDNA repair2012

Novel mutator mutants of E. coli nrdAB ribonucleotide reductase: insight into allosteric regulation and control of mutation rates.

Deepti Ahluwalia, Rachelle J Bienstock, Roel M Schaaper

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2012. 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
2.0field-weighted citation impact, top 14% 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, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor NProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Elevated Levels of the Escherichia coliJournal of bacteriology · 2021
    Article
  8. Genomic Changes and Genetic Divergence ofFrontiers in microbiology · 2021
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Basis of dATP inhibition of RNRs.The Journal of biological chemistry · 2018
    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 1 institution in 1 country.

Deepti AhluwaliaLaboratory of Molecular Genetics, National Institute of Environmental and Health Sciences, 111 TW Alexander Drive, Research Triangle Park, NC 27709, USA.
Rachelle J Bienstock
Roel M Schaaper
National Institute of Environmental Health Sciences · US

Funding

Mechanisms Of E. coli Replication FidelityZIAES065086 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI SCHAAPER, ROELAND · 2009 to 2025
$7.4M
MECHANISMS OF E COLI REPLICATION FIDELITYZ01ES065086 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI SCHAAPER, ROELAND · 1996 to 2008
$649k
Intramural NIH HHS Z01 ES065086Intramural NIH HHS ZIA ES065086
6 · The paper itself

Abstract

Ribonucleotide reductase (RNR) is the enzyme critically responsible for the production of the 5'-deoxynucleoside-triphosphates (dNTPs), the direct precursors for DNA synthesis. The dNTP levels are tightly controlled to permit high efficiency and fidelity of DNA synthesis. Much of this control occurs at the level of the RNR by feedback processes, but a detailed understanding of these mechanisms is still lacking. Using a genetic approach in the bacterium Escherichia coli, a paradigm for the class Ia RNRs, we isolated 23 novel RNR mutants displaying elevated mutation rates along with altered dNTP levels. The responsible amino-acid substitutions in RNR reside in three different regions: (i) the (d)ATP-binding activity domain, (ii) a novel region in the small subunit adjacent to the activity domain, and (iii) the dNTP-binding specificity site, several of which are associated with different dNTP pool alterations and different mutational outcomes. These mutants provide new insight into the precise mechanisms by which RNR is regulated and how dNTP pool disturbances resulting from defects in RNR can lead to increased mutation.

Indexed as

Mutation RateAllosteric RegulationDeoxyribonucleosidesEscherichia coliEscherichia coli ProteinsGene OrderModels, MolecularMutant ProteinsMutationProtein ConformationRibonucleoside Diphosphate ReductaseRibonucleotide ReductasesDeoxyribonucleosidesEscherichia coli ProteinsMutant ProteinsNrdA protein, E coliNrdB protein, E coliRibonucleoside Diphosphate ReductaseRibonucleotide Reductases

Identifiers

PMID22417940
PMCPMC3340444
OpenAlexW1991327687

What OpenQuestion holds

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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.