Evidence map›Paper›PMID 21338418›Full record

ArticleMolecular microbiology2011

The alternative aerobic ribonucleotide reductase of Escherichia coli, NrdEF, is a manganese-dependent enzyme that enables cell replication during periods of iron starvation.

Julia E Martin, James A Imlay

Open access · greenAbstract read
In one paragraph

Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

98 citing papers in PubMed, 143 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
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  6. Article
  7. The intricacies ofFrontiers in microbiology · 2025
    Review
  8. Article
  9. Review
  10. Microbes vary strategically in their metalation of mononuclear enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Manganese transporters regulate the resumption of replication in hydrogen peroxide-stressed Escherichia coli.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Article
  12. Article
  13. Review
  14. Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023
    Review
  15. Iron and copper onPeerJ · 2023
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

38 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Julia E MartinDepartment of Microbiology, University of Illinois, Urbana, IL 61801, USA.
James A Imlay
University of Illinois Urbana-Champaign · US

Funding

The Physiology of Oxidative Stress in Escherichia coliR01GM049640 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 1994 to 2024
$6.9M
Training Program in Chemistry-Interface with BiologyT32GM070421 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2005 to 2019
$5.4M
The Physiology of Oxidative Stress in Escherichia coliR37GM049640 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI IMLAY, JAMES A. · 2007 to 2016
$5.3M
NIGMS NIH HHS GM070421NIGMS NIH HHS GM49640NIGMS NIH HHS R01 GM049640NIGMS NIH HHS R37 GM049640NIGMS NIH HHS T32 GM070421
6 · The paper itself

Abstract

The genome of Escherichia coli encodes two class I ribonucleotide reductases. The first, NrdAB, is a well-studied iron-dependent enzyme that is essential for aerobic growth. The second, NrdEF, is not functional under routine conditions, and its role is obscure. Recent studies demonstrated that NrdEF can be activated in vitro by manganese as well as iron. Since iron enzymes are potential targets for hydrogen peroxide, and since the nrdHIEF operon is induced during H(2) O(2) stress, we hypothesized that H(2) O(2) might inactivate NrdAB and that NrdEF might be induced to compensate. This idea was tested using E. coli mutants that are chronically stressed by H(2) O(2) . Contrary to expectation, NrdAB remained active. Its resistance to H(2) O(2) depended upon YfaE, which helps to activate NrdB. The induction of NrdEF during H(2) O(2) stress was mediated by the inactivation of Fur, an iron-dependent repressor. This regulatory arrangement implied that NrdEF has a physiological role during periods of iron starvation. Indeed, NrdEF supported cell replication in iron-depleted cells. Iron bound to NrdF when it was expressed in iron-rich cells, but NrdEF was functional only in cells that were both iron-depleted and manganese-rich. Thus NrdEF supports DNA replication when iron is unavailable to activate the housekeeping NrdAB enzyme.

Indexed as

AerobiosisBacterial ProteinsDeoxyribonucleotidesDNAEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialHydrogen PeroxideIronManganeseOxidative StressRibonucleoside Diphosphate ReductaseRibonucleotide ReductasesBacterial ProteinsDeoxyribonucleotidesDNAEscherichia coli ProteinsHydrogen PeroxideIronManganeseNrdA protein, E coliNrdE protein, E coliNrdF protein, bacteriaRibonucleoside Diphosphate ReductaseRibonucleotide Reductases

Identifiers

PMID21338418
PMCPMC3097424
OpenAlexW2167456427

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.