Skip to main content
Article thumbnail
Location of Repository

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


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:
Provided by: e-Prints Soton

Suggested articles


  1. (1981). Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc Natl Acad Sci doi
  2. (1988). Binding site requirements for pea nuclear protein factor GT-1 correlate with sequences required for light-dependent transcriptional activation of the rbcS-3A gene.
  3. (2000). Gene regulation during late embryogenesis: the RY motif of maturation-specific gene promoters is a direct target of the FUS3 gene product. doi
  4. (2005). Monoterpene metabolism. Cloning, expression, and characterization of (-)-isopiperitenol/(-)-carveol dehydrogenase of peppermint and spearmint. doi
  5. (1987). Naturally occurring quinones III. Recent advances. doi
  6. (1997). Naturally occurring quinones IV. Recent advances. doi
  7. (1971). Naturally occurring quinones, 2 nd Edition. doi
  8. (2002). Regulation of gene expression by low levels of ultraviolet-B radiation in Pisum sativum: Isolation of novel genes by suppression subtractive hybridisation. doi
  9. (1997). Role of Arabidopsis MYC and MYB homologs in drought- and abscisic acid-regulated gene expression. doi
  10. (2001). Secoisolariciresinol dehydrogenase purification, cloning and functional expression.
  11. (1974). The middle ultraviolet reaching the ground. doi

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.