Polyamines: ubiquitous polycations with unique roles in growth and stress responses

Abstract

Background: Polyamines are small polycationic molecules found ubiquitously in all organisms and function in a wide variety of biological processes. In the past decade, molecular and genetic studies using mutants and transgenic plants with an altered activity of enzymes involved in polyamine biosynthesis have contributed much to a better understanding of the biological functions of polyamines in plants.

Possible roles: Spermidine is essential for survival of Arabidopsis embryos. One of the reasons may lie in the fact that spermidine serves as a substrate for the lysine hypusine post-translational modification of the eukaryotic translation initiation factor 5A, which is essential in all eukaryotic cells. Spermine is not essential but plays a role in stress responses, probably through the modulation of cation channel activities, and as a source of hydrogen peroxide during pathogen infection. Thermospermine, an isomer of spermine, is involved in stem elongation, possibly by acting on the regulation of upstream open reading frame-mediated translation.

Conclusions: The mechanisms of action of polyamines differ greatly from those of plant hormones. There remain numerous unanswered questions regarding polyamines in plants, such as transport systems and polyamine-responsive genes. Further studies on the action of polyamines will undoubtedly provide a new understanding of plant growth regulation and stress responses.

Fig. 1.

Biosynthetic pathways of polyamines in plants. Abbreviations: ACL5, ACAULIS5; ADC, arginine decarboxylase; AIH, agmatine iminohydrolase; CPA, N-carbamoylputrescine amidohydrolase; ODC, ornithine decarboxylase; SAMDC, S-adenosylmethionine decarboxylase; SPDS, spermidine synthase; SPMS, spermine synthase; TSPMS, thermospermine synthase.

Fig. 2.

Molecular phylogenetic tree of the amino acid sequences of spermidine/spermine synthase-related proteins. The full-length amino acid sequences were aligned by use of Clustal X and the tree was drawn by the neighbour-joining method with the software TreeView. ACL5 represents thermospermine synthase or its putative orthologues, which may have been acquired by an ancestor of the plant lineage through horizontal gene transfer from archaea or bacteria, as suggested by the absence of ACL5-like sequences in animals and fungi (Minguet et al., 2008). Abbreviations: PMT, putrescine N-methyltransferase; diatom, Thalassiosira pseudonana; moss, Physcomitrella patens; thermophile, Thermus thermophilus.

Fig. 3.

Phenotype of the Arabidopsis acl5-1 mutants, which are defective in the synthesis of thermospermine. Forty-day-old plants of acl5-1 (left) and transgenic acl5-1 expressing a full-length cDNA of the moss ACL5B (GenBank accession number EDQ54752) (right) are shown.