The biochemistry, genetics, and regulation of polyamine biosynthesis in Saccharomyces cerevisiae

Fed Proc. 1982 Dec;41(14):3084-8.


We have studied the enzymes and genes involved in the biosynthesis of putrescine, spermidine, and spermine in Saccharomyces cerevisiae. Mutants have been isolated with defects in the biosynthetic pathway as follows: spe10 mutants, deficient in ornithine decarboxylase, cannot make putrescine, spermidine, or spermine; spe2 mutants, lacking S-adenosylmethionine decarboxylase, cannot make spermidine or spermine; spe3 mutants, lacking putrescine aminopropyltransferase, cannot make spermidine or spermine; and spe4 and spe40 mutants, lacking spermidine aminopropyltransferase, contain no spermine and permit growth of spe10 mutants. Studies with these mutants have shown that in yeast: 1) polyamines are absolutely required for growth; 2) putrescine is formed only by decarboxylation or ornithine; 3) two separate aminopropyltransferases are required for spermidine and spermine synthesis; 4) spermine and spermidine are important in the regulation of ornithine decarboxylase and the amines exert this control by a posttranslational modification of the enzyme; and 5) spermidine or spermine is essential for sporulation of yeast and for the maintenance of the double-stranded RNA killer plasmid. Recent studies in amine-deficient mutants of Escherichia coli have shown an important role of the polyamines in protein synthesis in vivo.

MeSH terms

  • Adenosylmethionine Decarboxylase / genetics
  • Bacterial Proteins / biosynthesis
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Mutation
  • Ornithine Decarboxylase / genetics
  • Polyamines / biosynthesis*
  • Putrescine / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / physiology*
  • Spermidine Synthase / genetics


  • Bacterial Proteins
  • Polyamines
  • Spermidine Synthase
  • Ornithine Decarboxylase
  • Adenosylmethionine Decarboxylase
  • Putrescine