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

The Pisum sativum SAD short-chain dehydrogenase/reductase: quinone reduction, tissue distribution, and heterologous expression
The Pisum sativum SAD short-chain dehydrogenase/reductase: quinone reduction, tissue distribution, and heterologous expression
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.
0032-0889
Scherbak, Nikolai
2a0d908c-fd12-4645-bc73-add15701d763
Ala-Häivälä, Anneli
7fce88fb-30e9-4139-82ee-ea468dcc2a58
Brosché, Mikael
2aaed7ba-80dd-4f08-bde4-719a9e5bd71a
Böwer, Nathalie
0f335f21-46c0-4be9-b4b0-936a726b1d4e
Strid, Hilja
c404a646-02ae-4f7b-b48e-c42d6cdf476f
Gittins, John R.
c4d269cc-aae0-4182-bc81-78dc724f7d95
Grahn, Elin
26739227-1f02-4cbf-b137-9043d4e6f2ad
Eriksson, Leif A.
8928e169-6d2a-4b53-96fd-89bcaa52eca9
Strid, Åke
5291be25-7846-4524-b9cb-d4f0fc2504cc
Scherbak, Nikolai
2a0d908c-fd12-4645-bc73-add15701d763
Ala-Häivälä, Anneli
7fce88fb-30e9-4139-82ee-ea468dcc2a58
Brosché, Mikael
2aaed7ba-80dd-4f08-bde4-719a9e5bd71a
Böwer, Nathalie
0f335f21-46c0-4be9-b4b0-936a726b1d4e
Strid, Hilja
c404a646-02ae-4f7b-b48e-c42d6cdf476f
Gittins, John R.
c4d269cc-aae0-4182-bc81-78dc724f7d95
Grahn, Elin
26739227-1f02-4cbf-b137-9043d4e6f2ad
Eriksson, Leif A.
8928e169-6d2a-4b53-96fd-89bcaa52eca9
Strid, Åke
5291be25-7846-4524-b9cb-d4f0fc2504cc

Scherbak, Nikolai, Ala-Häivälä, Anneli, Brosché, Mikael, Böwer, Nathalie, Strid, Hilja, Gittins, John R., Grahn, Elin, Eriksson, Leif A. and Strid, Åke (2011) The Pisum sativum SAD short-chain dehydrogenase/reductase: quinone reduction, tissue distribution, and heterologous expression. Plant Physiology. (doi:10.1104/pp.111.173336). (PMID:21343423)

Record type: Article

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.

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Published date: 22 February 2011
Additional Information: Online First article

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Local EPrints ID: 175535
URI: http://eprints.soton.ac.uk/id/eprint/175535
ISSN: 0032-0889
PURE UUID: 365fb288-ca5a-4b2c-b81d-c73b499374b4

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Date deposited: 24 Feb 2011 09:34
Last modified: 09 Sep 2019 19:00

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