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Reconstitution of a bacterial/plant polyamine biosynthesis pathway in Saccharomyces cerevisiae.
Klein, R D; Geary, T G; Gibson, A S; Favreau, M A; Winterrowd, C A; Upton, S J; Keithly, J S; Zhu, G; Malmberg, R L; Martinez, M P; Yarlett, N.
Afiliación
  • Klein RD; Pharmacia and Upjohn, Animal Health Discovery Research, Kalamazoo, MI 49007, USA.
  • Geary TG; Pharmacia and Upjohn, Animal Health Discovery Research, Kalamazoo, MI 49007, USA.
  • Gibson AS; Pharmacia and Upjohn, Animal Health Discovery Research, Kalamazoo, MI 49007, USA.
  • Favreau MA; Pharmacia and Upjohn, Animal Health Discovery Research, Kalamazoo, MI 49007, USA.
  • Winterrowd CA; Pharmacia and Upjohn, Animal Health Discovery Research, Kalamazoo, MI 49007, USA.
  • Upton SJ; Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
  • Keithly JS; Wadsworth Center, NY State Department of Health, David Axelrod Institute, Albany, NY 12201-2002, USA.
  • Zhu G; Wadsworth Center, NY State Department of Health, David Axelrod Institute, Albany, NY 12201-2002, USA.
  • Malmberg RL; Botany Department, University of Georgia, Athens, GA 30602-7271, USA.
  • Martinez MP; Pace University, Haskins Laboratories, 41 Park Row, New York, NY 10038-1598, USA.
  • Yarlett N; Pace University, Haskins Laboratories, 41 Park Row, New York, NY 10038-1598, USA.
Microbiology (Reading) ; 145 ( Pt 2): 301-307, 1999 Feb.
Article en En | MEDLINE | ID: mdl-10075412
Polyamine synthesis in most organisms is initiated by the decarboxylation of ornithine to form putrescine via ornithine decarboxylase (ODC). Plants, some bacteria and some fungi and protozoa generate putrescine from arginine, via arginine decarboxylase (ADC) and agmatine ureohydrolase (AUH) or agmatine iminohydrolase. A polyamine-requiring strain of Saccharomyces cerevisiae with a mutation in the gene encoding ODC was transformed with plasmids bearing genes encoding Escherichia coli ADC and AUH. Transformants regained the ability to grow in the absence of exogenous polyamines and contained enzyme activities consistent with the presence of both prokaryotic enzymes. Similar results were obtained when a plasmid containing a gene encoding oat (Avena sativa L.) ADC was substituted for the E. coli gene. These data demonstrate the successful complementation of a yeast biosynthetic polyamine synthesis defect by genes encoding an alternative pathway found in bacteria; they also show that plant ADC can substitute for the bacterial enzyme in this pathway. The recombinant yeast provides a tool for the study of the functional properties of these enzymes and for discovery of compounds that specifically inhibit this pathway.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Poliaminas / Saccharomyces cerevisiae / Avena / Escherichia coli Idioma: En Revista: Microbiology (Reading) Asunto de la revista: MICROBIOLOGIA Año: 1999 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Poliaminas / Saccharomyces cerevisiae / Avena / Escherichia coli Idioma: En Revista: Microbiology (Reading) Asunto de la revista: MICROBIOLOGIA Año: 1999 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido