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THE PLANT CELL, Vol 8, Issue 1 69-80, Copyright © 1996 by American Society of Plant Biologists
A Maize Gene Encoding an NADPH Binding Enzyme Highly Homologous to Isoflavone Reductases Is Activated in Response to Sulfur Starvation
S. Petrucco, A. Bolchi, C. Foroni, R. Percudani, G. L. Rossi and S. Ottonello
Institute of Biochemical Sciences, University of Parma, I-43100 Parma, Italy
Sulfur nutrition plays an important role in the growth and development of
higher plants, and glutathione, the main storage form of reduced sulfur, is
involved in the response to a variety of stress conditions. The
identification of genes activated on sulfur starvation may thus provide
insights not only into the mechanisms of adaptation to nutrient limitation
but also into the response(s) to stress resulting from glutathione
depletion. By applying mRNA differential display analysis to a model system
of maize seedlings grown hydroponically under either sulfate-sufficient or
sulfate-deprived conditions, we isolated a novel gene that is selectively
induced both in roots and shoots in response to sulfur starvation. This
gene encodes a cytosolic, monomeric protein of 33 kD that selectively binds
NADPH. The predicted polypeptide is highly homologous (>70%) to
leguminous isoflavone reductases (IFRs), but the maize protein (IRL for
isoflavone reductase-like) belongs to a novel family of proteins present in
a variety of plants. Anti-IRL antibodies specifically recognize IFR
polypeptides, yet the maize protein is unable to use various isoflavonoids
as substrates. IRL expression is correlated closely to glutathione
availability: it is persistently induced in seedlings whose glutathione
content is about fourfold lower than controls, and it is down-regulated
rapidly when control levels of glutathione are restored. This
glutathione-dependent regulation indicates that maize IRL may play a
crucial role in the establishment of a thiol-independent response to
oxidative stress under glutathione shortage conditions.
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