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Plant Cell Reports

, Volume 29, Issue 9, pp 955–965 | Cite as

Characterization of five polyamine oxidase isoforms in Arabidopsis thaliana

  • Yoshihiro TakahashiEmail author
  • Runzi Cong
  • G. H. M. Sagor
  • Masaru Niitsu
  • Thomas Berberich
  • Tomonobu KusanoEmail author
Original Paper

Abstract

The genome of Arabidopsis thaliana contains five genes (AtPAO1 to AtPAO5) encoding polyamine oxidase (PAO) which is an enzyme responsible for polyamine catabolism. To understand the individual roles of the five AtPAOs, here we characterized their tissue-specific and space-temporal expression. AtPAO1 seems to have a specific function in flower organ. AtPAO2 was expressed in shoot meristem and root tip of seedlings, and to a higher extent in the later growth stage within restricted parts of the organs, such as shoot meristem, leaf petiole and also in anther. The expression of AtPAO3 was constitutive, but highest in flower organ. AtPAO3 promoter activity was detected in cotyledon, distal portion of root, boundary region of mature rosette leaf and in filaments of flower. AtPAO4 was expressed at higher level all over young seedlings including roots, and in the mature stage its expression was ubiquitous with rather lower level in stem. AtPAO5 expression was observed in the whole plant body throughout various growth stages. Its highest expression was in flowers, particularly in sepals, but not in petals. Furthermore, we determined the substrate specificity of AtPAO1 to AtPAO4. None of the AtPAO enzymes recognized putrescine (Put). AtPAO2 and AtPAO3 showed almost similar substrate recognition patterns in which the most preferable substrate is spermidine (Spd) followed by less specificity to other tetraamines tested. AtPAO4 seemed to be spermine (Spm)-specific. More interestingly, AtPAO1 preferred thermospermine (T-Spm) and norspermine (NorSpm) to Spm, but did not recognize Spd. Based on the results, the individual function of AtPAOs is discussed.

Keywords

A. thaliana Gene expression Polyamine oxidase Space-temporal expression Substrate specificity 

Abbreviations

AO

Amine oxidase

NorSpm

Norspermine

N1-AcSpm

N1-Acetylspermine

PAO

Polyamine oxidase

PCR

Polymerase chain reaction

Put

Putrescine

Spd

Spermidine

Spm

Spermine

T-Spm

Thermospermine

Notes

Acknowledgments

This work was supported in part by Grant-in-Aids from the Japan Society for the Promotion of Science (JSPS) to TK (21380063) and YT (21780087). TB was supported by a JSPS-BRIDGE fellowship (BR090101).

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Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  • Yoshihiro Takahashi
    • 1
    Email author
  • Runzi Cong
    • 1
  • G. H. M. Sagor
    • 1
  • Masaru Niitsu
    • 2
  • Thomas Berberich
    • 1
    • 3
  • Tomonobu Kusano
    • 1
    Email author
  1. 1.Laboratory of Plant Molecular and Cellular Biology, Graduate School of Life SciencesTohoku UniversitySendaiJapan
  2. 2.Faculty of Pharmaceutical SciencesJosai UniversitySakadoJapan
  3. 3.Biodiversity and Climate Research Center FrankfurtFrankfurtGermany

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