POLYAMINE OXIDASE 1 from rice (Oryza sativa) is a functional ortholog of arabidopsis POLYAMINE OXIDASE 5

Taibo Liu, Dong Wook Kim, Masaru Niitsu, Thomas Berberich, Tomonobu Kusano

    Research output: Contribution to journalArticlepeer-review

    15 Citations (Scopus)


    POLYAMINE OXIDASE 1 (OsPAO1), from rice (Oryza sativa), and POLYAMINE OXIDASE 5 (AtPAO5), from Arabidopsis (Arabidopsis thaliana), are enzymes sharing high identity at the amino acid level and with similar characteristics, such as polyamine specificity and pH preference; furthermore, both proteins localize to the cytosol. A loss-of-function Arabidopsis mutant, Atpao5-2, was hypersensitive to low doses of exogenous thermospermine but this phenotype could be rescued by introduction of the wild-type AtPAO5 gene. Introduction of OsPAO1, under the control of a constitutive promoter, into Atpao5-2 mutants also restored normal thermospermine sensitivity, allowing growth in the presence of low levels of thermospermine, along with a concomitant decrease in thermospermine content in plants. By contrast, introduction of OsPAO3, which encodes a peroxisome-localized polyamine oxidase, into Atpao5-2 plants could not rescue any of the mutant phenotypes in the presence of thermospermine. These results suggest that OsPAO1 is the functional ortholog of AtPAO5.

    Original languageEnglish
    Article numbere29773
    Pages (from-to)e29773-1-e29773-6
    JournalPlant Signaling and Behavior
    Issue numberJUL
    Publication statusPublished - 2014 Jul 25


    • Arabidopsis thaliana
    • AtPAO5
    • Oryza sativa
    • OsPAO1
    • Polyamine oxidase
    • Thermospermine

    ASJC Scopus subject areas

    • Plant Science


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