Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Physiology Preview
Published on June 15, 2006; 10.1104/pp.106.080911

This Article
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow All Versions of this Article:
141/4/1519    most recent
pp.106.080911v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (11)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tavladoraki, P.
Right arrow Articles by Federico, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tavladoraki, P.
Right arrow Articles by Federico, R.
Agricola
Right arrow Articles by Tavladoraki, P.
Right arrow Articles by Federico, R.

Received March 27, 2006
Returned for revision May 9, 2006
Accepted May 15, 2006

Heterologous Expression and Biochemical Characterization of a Polyamine Oxidase from Arabidopsis thaliana involved in Polyamine Back-Conversion

Paraskevi Tavladoraki *, Marianna Nicoletta Rossi , Giuseppe Saccuti , Miguel Angel Perez-Amador , Fabio Polticelli , Riccardo Angelini , and Rodolfo Federico

Department of Biology, University ‘Roma Tre’, 00146 Rome, Italy
Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia, Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain

* Corresponding author; email: tavlador{at}uniroma3.it.

Polyamine oxidase (PAO) is a FAD-dependent enzyme involved in polyamine catabolism. Animal PAO oxidize spermine or spermidine (and/or their acetyl derivatives) to produce H2O2, an aminoaldehyde and spermidine or putrescine, respectively, thus being involved in a polyamine back-conversion pathway. On the contrary, the plant PAO which have been characterized to date oxidize spermine and spermidine to produce 1,3-diaminopropane, H2O2 and an aminoaldehyde and are therefore involved in the terminal catabolism of polyamines. A database search within the Arabidopsis thaliana genome sequence showed the presence of a gene (AtPAO1) encoding for a putative PAO with 45% amino acid sequence identity with maize PAO. The AtPAO1 cDNA was isolated and cloned in a vector for heterologous expression in Escherichia coli. The recombinant protein was purified by affinity chromatography on guazatine-Sepharose 4B and was shown to be a flavoprotein able to oxidize spermine, norspermine and N 1-acetylspermine with a pH optimum at 8.0. Analysis of the reaction products showed that AtPAO1 produces spermidine from spermine and norspermidine from norspermine, demonstrating a substrate oxidation mode similar to that of animal PAO. To our knowledge, AtPAO1 is the first plant PAO reported to be involved in a polyamine back-conversion pathway.




This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
T. Kamada-Nobusada, M. Hayashi, M. Fukazawa, H. Sakakibara, and M. Nishimura
A Putative Peroxisomal Polyamine Oxidase, AtPAO4, is Involved in Polyamine Catabolism in Arabidopsis thaliana
Plant Cell Physiol., September 1, 2008; 49(9): 1272 - 1282.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2006 by the American Society of Plant Biologists