Polyamine biosynthetic diversity in plants and algae

Christine Fuell, Katherine A. Elliott, Colin C. Hanfrey, Marina Franceschetti, Anthony J. Michael

Research output: Contribution to journalArticlepeer-review

118 Scopus citations

Abstract

Polyamine biosynthesis in plants differs from other eukaryotes because of the contribution of genes from the cyanobacterial ancestor of the chloroplast. Plants possess an additional biosynthetic route for putrescine formation from arginine, consisting of the enzymes arginine decarboxylase, agmatine iminohydrolase and N-carbamoylputrescine amidohydrolase, derived from the cyanobacterial ancestor. They also synthesize an unusual tetraamine, thermospermine, that has important developmental roles and which is evolutionarily more ancient than spermine in plants and algae. Single-celled green algae have lost the arginine route and are dependent, like other eukaryotes, on putrescine biosynthesis from the ornithine. Some plants like Arabidopsis thaliana and the moss Physcomitrella patens have lost ornithine decarboxylase and are thus dependent on the arginine route. With its dependence on the arginine route, and the pivotal role of thermospermine in growth and development, Arabidopsis represents the most specifically plant mode of polyamine biosynthesis amongst eukaryotes. A number of plants and algae are also able to synthesize unusual polyamines such as norspermidine, norspermine and longer polyamines, and biosynthesis of these amines likely depends on novel aminopropyltransferases similar to thermospermine synthase, with relaxed substrate specificity. Plants have a rich repertoire of polyamine-based secondary metabolites, including alkaloids and hydroxycinnamic amides, and a number of polyamine-acylating enzymes have been recently characterised. With the genetic tools available for Arabidopsis and other model plants and algae, and the increasing capabilities of comparative genomics, the biological roles of polyamines can now be addressed across the plant evolutionary lineage.

Original languageEnglish (US)
Pages (from-to)513-520
Number of pages8
JournalPlant Physiology and Biochemistry
Volume48
Issue number7
DOIs
StatePublished - Jul 2010

Keywords

  • Aminopropyltransferase
  • Endosymbiotic
  • Hydroxycinnamoylspermidine
  • Polyamine
  • Siderophore
  • Thermospermine

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science

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