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, *
Article Information
Identifiers and Pagination:
Year: 2008Volume: 2
First Page: 183
Last Page: 189
Publisher ID: TOBIOTJ-2-183
DOI: 10.2174/1874070700802010183
Article History:
Received Date: 27/12/2007Revision Received Date: 02/06/2008
Acceptance Date: 10/06/2008
Electronic publication date: 2/7/2008
Collection year: 2008
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.
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.