REVIEW ARTICLE


Modulation of Polyamine Biosynthesis in Transformed Tobacco Plants by Targeting Ornithine Decarboxylase to an Atypical Subcellular Compartment



G. Nölke1, B. Schneider1, #, S. Agdour1, J. Drossard2, R. Fischer1, 2, S. Schillberg2, *
1 Institut für Molekulare Biotechnologie, RWTH Aachen, Germany
2 Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Germany and
# Present address: Biologische Bundesanstalt, Institut für Pflanzenschutz im Obstbau, Germany


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Creative Commons License
© 2008 Nölke et al.

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (https://creativecommons.org/licenses/by/4.0/legalcode). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

* Address correspondence to this author at the Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Germany; E-mail: stefan.schillberg@ime.fraunhofer.de


Abstract

Ornithine decarboxylase (ODC) is a cytosolic enzyme that catalyses the direct decarboxylation of L-ornithine to putrescine, one of the rate-limiting steps of polyamine biosynthesis in plants. We targeted recombinant human ODC to the cytosol and apoplast of transformed tobacco (Nicotiana tabacum) plants, and evaluated the impact of subcellular compartmentalization on the accumulation of the enzyme and its corresponding metabolic product. Immunoblot analysis showed that human ODC accumulated to high levels in both the cytosol and apoplast of transiently transformed tobacco leaves. In stably transformed tobacco plants with ODC targeted to the apoplast, enzyme activity increased by up to 32- fold (P < 0.001) and putrescine levels increased by up to 8.5-fold (P < 0.05) compared to wild type plants. These results demonstrate that the subcellular targeting of polyamine pathway enzymes may provide a useful strategy to enhance the accumulation and activity of enzymes involved in polyamine biosynthesis and may increase metabolic flux toward desired end products.

Keywords: metabolic engineering, polyamine metabolism, recombinant enzyme, subcellular targeting, transgenic plants.