Evidence map›Paper›PMID 15629931›Full record

ArticleJournal of bacteriology2005

Roles of thioredoxin reductase during the aerobic life of Lactococcus lactis.

Karin Vido, Hélène Diemer, Alain Van Dorsselaer, Emmanuelle Leize, Vincent Juillard, Alexandra Gruss, Philippe Gaudu

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 17% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Modulating the microbiome as an approach to anticancer drug development.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Frontiers in microbiology · 2021
    Article
  9. Article
  10. Higher nisin yield is reached with glutathione and pyruvate compared with heme in Lactococcus lactis N8.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020
    Article
  11. Article
  12. NADH peroxidase plays a crucial role in consuming HBioscience of microbiota, food and health · 2020
    Article
  13. Review
  14. Adaptation to Aerobic Environment ofFrontiers in microbiology · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 2 institutions in 1 country.

Karin VidoUnité de Recherches Laitières et Génétique Appliquée, INRA, Domaine de Vilvert, 78352 Jouy en Josas, France.
Hélène Diemer
Alain Van Dorsselaer
Emmanuelle Leize
Vincent Juillard
Alexandra Gruss
Philippe Gaudu
Université de Strasbourg · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thiol-disulfide bond balance is generally maintained in bacteria by thioredoxin reductase-thioredoxin and/or glutathione-glutaredoxin systems. Some gram-positive bacteria, including Lactococcus lactis, do not produce glutathione, and the thioredoxin system is presumed to be essential. We constructed an L. lactis trxB1 mutant. The mutant was obtained under anaerobic conditions in the presence of dithiothreitol (DTT). Unexpectedly, the trxB1 mutant was viable without DTT and under aerated static conditions, thus disproving the essentiality of this system. Aerobic growth of the trxB1 mutant did not require glutathione, also ruling out the need for this redox maintenance system. Proteomic analyses showed that known oxidative stress defense proteins are induced in the trxB1 mutant. Two additional effects of trxB1 were not previously reported in other bacteria: (i) induction of proteins involved in fatty acid or menaquinone biosynthesis, indicating that membrane synthesis is part of the cellular response to a redox imbalance, and (ii) alteration of the isoforms of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GapB). We determined that the two GapB isoforms in L. lactis differed by the oxidation state of catalytic-site cysteine C152. Unexpectedly, a decrease specific to the oxidized, inactive form was observed in the trxB1 mutant, possibly because of proteolysis of oxidized GapB. This study showed that thioredoxin reductase is not essential in L. lactis and that its inactivation triggers induction of several mechanisms acting at the membrane and metabolic levels. The existence of a novel redox function that compensates for trxB1 deficiency is suggested.

Indexed as

AerobiosisBacterial ProteinsCell MembraneDithiothreitolElectrophoresis, Gel, Two-DimensionalGenes, BacterialGlutathioneGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)IsoenzymesLactococcus lactisMutationOxidation-ReductionProteomeThioredoxin-Disulfide ReductaseBacterial ProteinsDithiothreitolGlutathioneGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)IsoenzymesProteomeThioredoxin-Disulfide Reductase

Identifiers

PMID15629931
PMCPMC543548
OpenAlexW2159342900

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.