Polyamines: Small Molecules Triggering Pathways in Plant Growth and Development

Walden, Richard; Cordeiro, A. R.; Tiburcio, Antonio F.

doi:10.1104/pp.113.4.1009

Cited by 313 publications

(199 citation statements)

References 22 publications

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“…In higher plants, putrescine might be more related to root initiation [53], even though controversy exists [20,54]. Our findings that bud2 plants contain more putrescine and have the enhanced root growth appear to support the argument that putrescine has a promotive effect on root growth.…”

Section: Roles Of Plant Polyaminessupporting

confidence: 72%

BUD2, encoding an S-adenosylmethionine decarboxylase, is required for Arabidopsis growth and development

et al. 2006

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Polyamines are implicated in regulating various developmental processes in plants, but their exact roles and how they govern these processes still remain elusive. We report here an Arabidopsis bushy and dwarf mutant, bud2, which results from the complete deletion of one member of the small gene family that encodes S-adenosylmethionine decarboxylases (SAMDCs) necessary for the formation of the indispensable intermediate in the polyamine biosynthetic pathway. The bud2 plant has enlarged vascular systems in inflorescences, roots, and petioles, and an altered homeostasis of polyamines. The double mutant of bud2 and samdc1, a knockdown mutant of another SAMDC member, is embryo lethal, demonstrating that SAMDCs are essential for plant embryogenesis. Our results suggest that polyamines are required for the normal growth and development of higher plants.Cell Research (2006) IntroductionPolyamines, including diamine putrescine, triamine spermidine and tetraamine spermine, are aliphatic nitrogen compounds distributed widely from bacteria to higher plants [1,2] and have been implicated to play important roles in growth and development [3]. At the cellular level, polyamines are organic cations, interacting with the macromolecules that possess anionic groups such as DNA, RNA, lipids and proteins, thereby influencing DNA conformation, gene expression and protein synthesis, and modulating enzyme activity. In higher plants, polyamines are able to affect membrane fluidity by binding to phospholipids in membrane [4] and mediate biotic and abiotic stress responses, such as pathogen infection, osmotic stress, potassium deficiency and wounding [5][6][7][8][9]. Previous observations revealed that polyamines may be involved in a variety of plant developmental processes, such as cell division, root initiation, somatic embryogenesis, xylogenesis, flower development, fruit ripening and senescence [3]. Recent studies have indicated that polyamines also affect the formation of plant architecture, such as internode elongation [10,11], root branching [12] and shoot apical dominance [13].The plant polyamine biosynthetic pathway is relatively simple [14]. Putrescine is derived either from ornithine catalyzed by ornithine decarboxylase (ODC) or from arginine through several steps catalyzed by arginine decarboxylase (ADC), agmatine iminohydrolase and N-carbamoylputrescine amidohydrolase. Spermidine and spermine are synthesized from putrescine through spermidine and spermine synthases (SPDS and SPMS) from the donor of decarboxylated S-adenosylmethionine (dcSAM), which is produced from S-adenosylmethionine (SAM) by the action of S-adenosylmethionine decarboxylase (SAMDC).Although application of inhibitors is very useful in studying the polyamine biosynthetic pathway and in ex- [11,[19][20][21][22][23][24]. However, no mutant defective in SAMDC has been reported yet, although SAMDC cDNAs were cloned and their transgenic plants have been generated [25][26][27][28][29]. In this paper, we report the isolation and characterization of an Arabidopsis...

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Section: Roles Of Plant Polyaminessupporting

confidence: 72%

BUD2, encoding an S-adenosylmethionine decarboxylase, is required for Arabidopsis growth and development

et al. 2006

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“…The second nuclear gene, SAM, is part of an essential plant biochemical pathway and is involved in the biosynthesis of polyamines and the phytohormone ethylene (37). We expect that this gene could be under selection, which could distort the topography of the haplotype network from that of the neutral gene network, yet it also carries the signature of multiple gene pools associated with separate domestications.…”

Section: Distribution Of Genetic Diversitymentioning

confidence: 99%

Phylogeography of Asian wild rice, Oryza rufipogon , reveals multiple independent domestications of cultivated rice, Oryza sativa

Londo

Chiang

Hung

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

615

466

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Cultivated rice, Oryza sativa L., represents the world's most important staple food crop, feeding more than half of the human population. Despite this essential role in world agriculture, the history of cultivated rice's domestication from its wild ancestor, Oryza rufipogon, remains unclear. In this study, DNA sequence variation in three gene regions is examined in a phylogeographic approach to investigate the domestication of cultivated rice. Results indicate that India and Indochina may represent the ancestral center of diversity for O. rufipogon. Additionally, the data suggest that cultivated rice was domesticated at least twice from different O. rufipogon populations and that the products of these two independent domestication events are the two major rice varieties, Oryza sativa indica and Oryza sativa japonica. Based on this geographical analysis, O. sativa indica was domesticated within a region south of the Himalaya mountain range, likely eastern India, Myanmar, and Thailand, whereas O. sativa japonica was domesticated from wild rice in southern China.

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“…This function is still unknown. Among plant physiologists, the suspected but unknown roles of spermidine in plant growth and development are controversially discussed (52)(53)(54)(55). The requirement of spermidine as an essential substrate for deoxyhypusine formation provides direct evidence for a function of this polyamine in plant metabolism.…”

Section: Assaymentioning

confidence: 99%

Deoxyhypusine Synthase from Tobacco

Ober

Hartmann

1999

Journal of Biological Chemistry

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Deoxyhypusine synthase catalyzes the formation of a deoxyhypusine residue in the translation eukaryotic initiation factor 5A (eIF5A) precursor protein by transferring an aminobutyl moiety from spermidine onto a conserved lysine residue within the eIF5A polypeptide chain. This reaction commences the activation of the initiation factor in fungi and vertebrates. A mechanistically identical reaction is known in the biosynthetic pathway leading to pyrrolizidine alkaloids in plants. Deoxyhypusine synthase from tobacco was cloned and expressed in active form in Escherichia coli. It catalyzes the formation of a deoxyhypusine residue in the tobacco eIF5A substrate as shown by gas chromatography coupled with a mass spectrometer. The enzyme also accepts free putrescine as the aminobutyl acceptor, instead of lysine bound in the eIF5A polypeptide chain, yielding homospermidine. Conversely, it accepts homospermidine instead of spermidine as the aminobutyl donor, whereby the reactions with putrescine and homospermidine proceed at the same rate as those involving the authentic substrates. The conversion of deoxyhypusine synthase-catalyzed eIF5A deoxyhypusinylation pinpoints a function for spermidine in plant metabolism. Furthermore, and quite unexpectedly, the substrate spectrum of deoxyhypusine synthase hints at a biochemical basis behind the sparse and skew occurrence of both homospermidine and its pyrrolizidine derivatives across distantly related plant taxa.The eukaryotic initiation factor 5A (eIF5A), 1 a small 17.4-kDa protein, is activated by a post-translational modification of a specific lysine residue to hypusine (N ⑀ -(4-amino-2-hydroxybutyl)lysine) in an enzyme-catalyzed two-step mechanism (reviewed in Refs. 1 and 2). In the first step, the aminobutyl moiety of the polyamine spermidine is transferred by deoxyhypusine synthase (EC 1.1.1.249) in an NAD ϩ -dependent reaction to the ⑀-amino group of a specific lysine residue in the eIF5A precursor protein to form deoxyhypusine. In the second step, deoxyhypusine hydroxylase (EC 1.14.99.29) catalyzes the hydroxylation of the deoxyhypusine residue to hypusine. Activated eIF5A is the only protein in which the unusual amino acid hypusine has been detected to date (3, 4), the modification is one of the most specific post-translational modifications known (5, 6). eIF5A seems to be ubiquitous among eukaryotes (7) and archaebacteria (8). Its amino acid sequence is highly conserved, and the 12 amino acids surrounding the hypusine residue are identical in all eukaryotes studied. Although known for nearly 2 decades, the function of eIF5A is still obscure. Because of its in vitro activity in stimulating methionyl puromycin synthesis (9), eIF5A was classified as a protein synthesis initiation factor, though subsequent doubts have arisen as to whether initiation of protein synthesis is a major function of this protein (2). Using a yeast mutant, it was shown that depletion of eIF5A causes an immediate inhibition of cell growth but only a moderate inhibition (30%) of total protein synthe...

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Polyamines: Small Molecules Triggering Pathways in Plant Growth and Development

Cited by 313 publications

References 22 publications

BUD2, encoding an S-adenosylmethionine decarboxylase, is required for Arabidopsis growth and development

BUD2, encoding an S-adenosylmethionine decarboxylase, is required for Arabidopsis growth and development

Phylogeography of Asian wild rice, Oryza rufipogon , reveals multiple independent domestications of cultivated rice, Oryza sativa

Deoxyhypusine Synthase from Tobacco

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