Evidence map›Paper›PMID 14617780›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase.

Manas K Chattopadhyay, Celia White Tabor, Herbert Tabor

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

46 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Engineering small peptide secretion inFrontiers in bioengineering and biotechnology · 2026
    Article
  4. Review
  5. Article
  6. Article
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  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Polyamine catabolism and oxidative damage.The Journal of biological chemistry · 2018
    Review
  18. Roles of polyamines in translation.The Journal of biological chemistry · 2018
    Review
  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 2 institutions in 1 country.

Manas K ChattopadhyayLaboratory of Biochemistry and Genetics, Building 8, Room 223, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Celia White Tabor
Herbert Tabor
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Polyamine Biosynthesis And Physiological FunctionsZIADK024709 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TABOR, HERBERT · 2009 to 2020
$4.9M
Polyamine Biosynthesis And MetabolismZ01DK024709 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TABOR, HERBERT · 1986 to 2008
$472k
6 · The paper itself

Abstract

In our earlier work we showed that either spermidine or spermine could support the growth of spe2Delta or spe3Delta polyamine-requiring mutants, but it was unclear whether the cells had a specific requirement for either of these amines. In the current work, we demonstrate that spermidine is specifically required for the growth of Saccharomyces cerevisiae. We were able to show this specificity by using a spe3Delta fms1Delta mutant that lacked both spermidine synthase and the FMS1-encoded amine oxidase that oxidizes spermine to spermidine. The polyamine requirement for the growth of this double mutant could only be satisfied by spermidine; i.e., spermine was not effective because it cannot be oxidized to spermidine in the absence of the FMS1 gene. We also showed that at least one of the reasons for the absolute requirement for spermidine for growth is the specificity of its function as a necessary substrate for the hypusine modification of eIF5A. Spermine itself cannot be used for the hypusine modification, unless it is oxidized to spermidine by the Fms1 amine oxidase. We have quantified the conversion of spermine in vivo and have shown that this conversion is markedly increased in a strain overexpressing the Fms1 protein. We have also shown this conversion in enzymatic studies by using the purified amine oxidase from yeast.

Indexed as

RNA-Binding ProteinsBase SequenceDNA, FungalEukaryotic Translation Initiation Factor 5AGenes, FungalKineticsLysineMutationOxidoreductases Acting on CH-NH Group DonorsPeptide Initiation FactorsPolyamine OxidaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpermidineSpermineSubstrate SpecificityDNA, FungalEukaryotic Translation Initiation Factor 5AFMS1 protein, S cerevisiaehypusineLysineOxidoreductases Acting on CH-NH Group DonorsPeptide Initiation FactorsPolyamine OxidaseRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSpermidineSpermine

Identifiers

PMID14617780
PMCPMC283513
OpenAlexW2160730455

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.