Plant and Cell Physiology Advance Access published online on August 14, 2008
Plant and Cell Physiology, doi:10.1093/pcp/pcn114
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
A putative peroxisomal polyamine oxidase, AtPAO4, is involved in the polyamine catabolism in Arabidopsis thaliana
1Division of Cell Mechanisms, Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan
2Department of Molecular Biomechanics, School of Life Science, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan
3RIKEN Plant Science Center, Tsurumi, Yokohama 230-0045, Japan
Corresponding author: Mikio Nishimura, Division of Cell Mechanisms, Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan, Phone: 81-564-55-7500; Fax: 81-564-55-7505; E-mail: mikosome{at}nibb.ac.jp
| Abstract |
|---|
We characterized three Arabidopsis polyamine oxidase genes, AtPAO2 , AtPAO3 and AtPAO4. Transient expressions of these genes as monomeric red fluorescent protein-fusion proteins in Arabidopsis root cells revealed that all are peroxisomal proteins. Quantitative analysis of their transcripts in various organs suggested that AtPAO4 is the major isoform in root peroxisomes. Analysis of recombinant AtPAO4 protein indicated that it is a flavoprotein that catalyzed the oxidative conversion of spermine to spermidine. AtPAO4 –deficient mutants established by using T-DNA insertion and RNA interference techniques had markedly increased spermine and decreased spermidine levels in the roots. These results suggest that AtPAO4 is a root peroxisomal polyamine oxidase that participates in polyamine catabolism. Microarray analysis showed that AtPAO4 -deficiency induced alterations in the expression of genes related to the drought stress response and flavonoid biosynthesis.
Keywords: Arabidopsis - peroxisome - polyamine - polyamine oxidase - spermidine - spermine
(Received July 20, 2008; Accepted August 5, 2008)
![]()
CiteULike
Connotea
Del.icio.us What's this?