Molecular evolution of n-methylputrescine oxidase in Tobacco

Maliwan Naconsie, Keita Kato, Tsubasa Shoji, Takashi Hashimoto*

*この論文の責任著者

研究成果: ジャーナルへの寄稿学術論文査読

50 被引用数 (Scopus)

抄録

Biosynthesis of nicotine in tobacco requires N-methylputrescine oxidase (MPO), which belongs to the copper-containing amine oxidase superfamily. Previous studies identified tobacco MPO1 and its close homolog NtDAO1 (formerly called MPO2), of which MPO1 has been shown preferentially to oxidize N-methylated amines. We show here that NtDAO1, as well as a homologous Arabidopsis diamine oxidase (DAO), accept non-N-methylated amines more efficiently than their corresponding N-methylated amines. MPO1 is coordinately regulated with other nicotine biosynthesis genes with regard to COI1-MYC2-dependent jasmonate induction and its dependence on nicotine-specific ERF transcription factors, whereas NtDAO1 is constitutively expressed at low basal levels in tobacco plants. Both MPO1 and NtDAO1 are targeted to peroxisomes by their C-terminal motifs, and the peroxisomal localization of MPO1 is required for it to function in nicotine biosynthesis in jasmonate-elicited cultured tobacco cells. Restricted occurrence of the MPO subfamily in Nicotiana and Solanum indicates that, during the formation of the Solanaceae, MPO has evolved from a DAO, which functions in polyamine catabolism within peroxisomes, by optimizing substrate preference and gene expression patterns to be suitable for alkaloid formation.

本文言語英語
ページ(範囲)436-444
ページ数9
ジャーナルPlant and Cell Physiology
55
2
DOI
出版ステータス出版済み - 2014/02

ASJC Scopus 主題領域

  • 生理学
  • 植物科学
  • 細胞生物学

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