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The Pisum sativum SAD short-chain dehydrogenase/reductase: quinone reduction, tissue distribution, and heterologous expression

By Nikolai Scherbak, Anneli Ala-Häivälä, Mikael Brosché, Nathalie Böwer, Hilja Strid, John R. Gittins, Elin Grahn, Leif A. Eriksson and Åke Strid

Abstract

The pea (Pisum sativum) tetrameric short-chain alcohol dehydrogenase-like protein (SAD) family consists of at least three highly similar members (SAD-A, -B, and -C). According to mRNA data, environmental stimuli induce SAD expression (Brosché and Strid (1999) Plant Physiol 121: 479-487). The aim of this study was to characterize the SAD proteins by examining their catalytic function, distribution in pea, and induction in different tissues. In enzyme activity assays using a range of potential substrates, the SAD-C enzyme was shown to reduce one- or two-ring membered quinones lacking long hydrophobic hydrocarbon tails. Immunological assays using a specific antiserum against the protein, demonstrated that different tissues and cell types were shown to contain small amounts of SAD protein that was predominantly located within epidermal or sub-epidermal cells and around vascular tissue. Particularly high local concentrations were observed in the protoderm of the seed cotyledonary axis. Two bow-shaped rows of cells in the ovary and the placental surface facing the ovule also exhibited considerable SAD staining. UV-B irradiation led to increased staining in epidermal and sub-epidermal cells of leaves and stems. The different localization patterns of SAD suggest functions in both development and in responses to environmental stimuli. Finally, the pea SAD-C promoter was shown to confer heterologous wound-induced expression in Arabidopsis thaliana, which confirmed that the inducibility of its expression is regulated at the transcriptional level

Topics: QH301
Year: 2011
OAI identifier: oai:eprints.soton.ac.uk:175535
Provided by: e-Prints Soton

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Citations

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