Evidence map›Paper›PMID 25893566›Full record

ArticleCurrent genetics2015

Serine hydroxymethyltransferase: a key player connecting purine, folate and methionine metabolism in Saccharomyces cerevisiae.

Christelle Saint-Marc, Hans C Hürlimann, Bertrand Daignan-Fornier, Benoît Pinson

Abstract read
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Article in Current genetics, 2015. 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
0.8field-weighted citation impact, top 28% 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, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Dual control of NADeLife · 2019
    Article
  5. Article
  6. The role of yeast mCurrent genetics · 2018
    Review
  7. The mCurrent genetics · 2018
    Review
  8. 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

4 authors at 1 institution in 2 countries.

Christelle Saint-MarcUMR 5095, Institut de Biochimie et Génétique Cellulaires (IBGC), Université de Bordeaux, 1 rue Camille Saint-Saëns, 33077, Bordeaux, France.
Hans C HürlimannUMR 5095, Institut de Biochimie et Génétique Cellulaires (IBGC), Université de Bordeaux, 1 rue Camille Saint-Saëns, 33077, Bordeaux, France.
Bertrand Daignan-FornierUMR 5095, Institut de Biochimie et Génétique Cellulaires (IBGC), Université de Bordeaux, 1 rue Camille Saint-Saëns, 33077, Bordeaux, France. b.daignan-fornier@ibgc.cnrs.fr.
Benoît PinsonUMR 5095, Institut de Biochimie et Génétique Cellulaires (IBGC), Université de Bordeaux, 1 rue Camille Saint-Saëns, 33077, Bordeaux, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous genetic analyses showed phenotypic interactions between 5-amino-4-imidazole carboxamide ribonucleotide 5'-phosphate (AICAR) produced from the purine and histidine pathways and methionine biosynthesis. Here, we revisited the effect of AICAR on methionine requirement due to AICAR accumulation in the presence of the fau1 mutation invalidating folinic acid remobilization. We found that this methionine auxotrophy could be suppressed by overexpression of the methionine synthase Met6 or by deletion of the serine hydroxymethyltransferase gene SHM2. We propose that in a fau1 background, AICAR, by stimulating the transcriptional expression of SHM2, leads to a folinic acid accumulation inhibiting methionine synthesis by Met6. In addition, we uncovered a new methionine auxotrophy for the ade3 bas1 double mutant that can be rescued by overexpressing the SHM2 gene. We propose that methionine auxotrophy in this mutant is the result of a competition for 5,10-methylenetetrahydrofolate between methionine and deoxythymidine monophosphate synthesis. Altogether, our data show intricate genetic interactions between one-carbon units, purine and methionine metabolism through fine-tuning of serine hydroxymethyltransferase by AICAR and the transcription factor Bas1.

Indexed as

Gene Expression Regulation, Fungal5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseAminoimidazole CarboxamideCarbon-Nitrogen LigasesFolic AcidGlycine HydroxymethyltransferaseHistidineLeucovorinMethionineMutationPurinesRibonucleotidesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTetrahydrofolatesThymidine5,10-methenyltetrahydrofolate synthetase5,10-methylenetetrahydrofolic acid5-Methyltetrahydrofolate-Homocysteine S-MethyltransferaseAICA ribonucleotideAminoimidazole CarboxamideBAS1 protein, S cerevisiaeCarbon-Nitrogen LigasesFolic AcidGlycine HydroxymethyltransferaseHistidineLeucovorinMethioninePurinesRibonucleotidesSaccharomyces cerevisiae ProteinsTetrahydrofolatesThymidineTrans-ActivatorsAICARAmino acidsCross-pathway regulationNucleotidesOne-carbon unitsSerine hydroxymethyltransferase

Identifiers

PMID25893566
OpenAlexW2082750628

What OpenQuestion holds

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Registered trials

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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.