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

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

Abstract

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

Substances

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