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Published on June 26, 2008; 10.1104/pp.108.123802

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Received May 31, 2008
Accepted June 18, 2008

Bridging The Gap Between Plant And Mammalian Polyamine Catabolism: A Novel Peroxisomal Polyamine Oxidase Responsible For A Full Back-Conversion Pathway In Arabidopsis thaliana

Panagiotis N. Moschou , Maite Sanmartin , Athina H. Andriopoulou , Enrique Rojo , Jose J. Sanchez-Serrano , and Kalliopi A. Roubelakis-Angelakis *

Department of Biology, University of Crete, P.O. Box 2208, 71409, Heraklion, Greece; Centro Nacional de Biotecnologia-CSIC, Campus de Cantoblanco UAM 28049, Madrid, Spain

* Corresponding author; email: poproube{at}biology.uoc.gr.

In contrast to animals, where polyamine (PA) catabolism efficiently converts Spermine (Spm) to Putrescine (Put), plants have been considered to possess a polyamine catabolic pathway producing 1,3-diaminopropane (1,3-Dap), {Delta}1-pyrroline, the corresponding aldehyde and H2O2, but unable to back-convert Spm to Put. Arabidopsis thaliana genome contains at least five putative polyamine oxidase (PAO) members, with yet unknown localization and physiological role(s). Recently, Tavladoraki et al., (2006) identified AtPAO1 as an enzyme similar to the mammalian Spm oxidase (SMO), which converts Spm to Spermidine (Spd). In this work we have performed in silico analysis of the five Arabidopsis thaliana genes and have identified Polyamine Oxidase 3 (AtPAO3) as a non-typical Polyamine Oxidase (PAO) in terms of homology, compared to other known PAOs. We have expressed the gene AtPAO3 and have purified a protein corresponding to it, using the inducible heterologous expression system of Escherichia coli. AtPAO3 catalyzed the sequential conversion/oxidation of Spm to Spd, and of Spd to Put, thus exhibiting functional homology to the mammalian PAOs. The best substrate for this pathway was Spd, whereas the N1-acetyl-derivatives of Spm and Spd were oxidized less efficiently. On the other hand, no activity was detected when diamines (Agmatine, Cadaverine and Put) were used as substrates. Moreover, although AtPAO3 does not exhibit significant similarity to the other known PAOs, it is efficiently inhibited by guazatine, a potent PAO inhibitor. AtPAO3 contains a peroxisomal targeting motif at the C-terminus, and it targets Green Fluorescence Protein (GFP) to peroxisomes when fused at the N-terminus but not at the C-terminus. These results reveal that AtPAO3 is a peroxisomal protein and that the C-terminus of the protein contains the sorting information. The overall data reinforce the view that plants and mammals possess a similar PA oxidation system, concerning both the subcellular localization and the mode of its action.




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P. N. Moschou, P. F. Sarris, N. Skandalis, A. H. Andriopoulou, K. A. Paschalidis, N. J. Panopoulos, and K. A. Roubelakis-Angelakis
Engineered Polyamine Catabolism Preinduces Tolerance of Tobacco to Bacteria and Oomycetes
Plant Physiology, April 1, 2009; 149(4): 1970 - 1981.
[Abstract] [Full Text] [PDF]


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