Evidence map›Paper›PMID 25745108›Full record

ArticleThe Journal of biological chemistry2015

Trans-sulfuration Pathway Seleno-amino Acids Are Mediators of Selenomethionine Toxicity in Saccharomyces cerevisiae.

Myriam Lazard, Marc Dauplais, Sylvain Blanquet, Pierre Plateau

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
4.6field-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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.

  1. Pooled it
  2. Review
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  4. Review
  5. Article
  6. Article
  7. Review
  8. Biosynthesis, Engineering, and Delivery of Selenoproteins.International journal of molecular sciences · 2023
    Review
  9. Recoding UAG to selenocysteine inRNA (New York, N.Y.) · 2023
    Article
  10. Review
  11. Article
  12. Article
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  15. Article
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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

4 authors at 2 institutions in 1 country.

Myriam LazardFrom the Ecole Polytechnique, Laboratoire de Biochimie, CNRS, 91128 Palaiseau Cedex, France myriam.lazard@polytechnique.edu.
Marc DauplaisFrom the Ecole Polytechnique, Laboratoire de Biochimie, CNRS, 91128 Palaiseau Cedex, France.
Sylvain BlanquetFrom the Ecole Polytechnique, Laboratoire de Biochimie, CNRS, 91128 Palaiseau Cedex, France.
Pierre PlateauFrom the Ecole Polytechnique, Laboratoire de Biochimie, CNRS, 91128 Palaiseau Cedex, France.
Centre National de la Recherche Scientifique · FRÉcole Polytechnique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Toxicity of selenomethionine, an organic derivative of selenium widely used as supplement in human diets, was studied in the model organism Saccharomyces cerevisiae. Several DNA repair-deficient strains hypersensitive to selenide displayed wild-type growth rate properties in the presence of selenomethionine indicating that selenide and selenomethionine exert their toxicity via distinct mechanisms. Cytotoxicity of selenomethionine decreased when the extracellular concentration of methionine or S-adenosylmethionine was increased. This protection resulted from competition between the S- and Se-compounds along the downstream metabolic pathways inside the cell. By comparing the sensitivity to selenomethionine of mutants impaired in the sulfur amino acid pathway, we excluded a toxic effect of Se-adenosylmethionine, Se-adenosylhomocysteine, or of any compound in the methionine salvage pathway. Instead, we found that selenomethionine toxicity is mediated by the trans-sulfuration pathway amino acids selenohomocysteine and/or selenocysteine. Involvement of superoxide radicals in selenomethionine toxicity in vivo is suggested by the hypersensitivity of a Δsod1 mutant strain, increased resistance afforded by the superoxide scavenger manganese, and inactivation of aconitase. In parallel, we showed that, in vitro, the complete oxidation of the selenol function of selenocysteine or selenohomocysteine by dioxygen is achieved within a few minutes at neutral pH and produces superoxide radicals. These results establish a link between superoxide production and trans-sulfuration pathway seleno-amino acids and emphasize the importance of the selenol function in the mechanism of organic selenium toxicity.

Indexed as

Amino Acids, SulfurDietary SupplementsDNA RepairHumansMetabolic Networks and PathwaysMethionineMutationOxidative StressSaccharomyces cerevisiaeS-AdenosylmethionineSelenious AcidSelenium CompoundsSelenocysteineSelenomethionineAmino Acids, SulfurMethionineS-AdenosylmethionineSelenious AcidSelenium CompoundsSelenocysteineselenolSelenomethionineselenomethylselenocysteineReactive Oxygen Species (ROS)SeleniumSelenocysteineSelenomethionineSuperoxide IonToxicityYeast Metabolism

Identifiers

PMID25745108
PMCPMC4409240
OpenAlexW2090911691

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.