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Plant and Cell Physiology Advance Access published online on February 5, 2007
Plant and Cell Physiology, doi:10.1093/pcp/pcm018
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© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Molecular Cloning of N-methylputrescine Oxidase from Tobacco

Akira Katoh, Tsubasa Shoji and Takashi Hashimoto

Nara Institute of Science and Technology, Graduate School of Biological Sciences, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan

Corresponding author: Dr. Takashi Hashimoto, Nara Institute of Science and Technology, Graduate School of Biological Sciences, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan, Tel: 0743-72-5520, Fax: 0743-72-5529, e-mail: hasimoto{at}bs.naist.jp


  Abstract

Nicotine biosynthesis in Nicotiana species requires an oxidative deamination of N-methylputrescine, catalyzed by N-methylputrescine oxidase (MPO). In a screen for tobacco genes that were down-regulated in a tobacco mutant with altered regulation of nicotine biosynthesis, we identified two homologous MPO cDNAs which encode diamine oxidases of a particular subclass. Tobacco MPO genes were expressed specifically in the root, and up-regulated by jasmonate treatment. Recombinant MPO protein expressed in E. coli formed a homo-dimer and deaminated N-methylputrescine more efficiently than symmetrical diamines. These results indicate that MPO evolved from general diamine oxidases to function effectively in nicotine biosynthesis.

Keywords: diamine oxidase - Nicotiana tabacum (tobacco) - nicotine – N-methylputrescine

The nucleotide sequences reported in this paper have been deposited in the DDBJ/EMBL/GenBank database under accession numbers AB289456 [GenBank] and AB289457 [GenBank] .


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