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PLANT PHYSIOLOGY , Vol 115, Issue 4 1721-1727, Copyright © 1997 by American Society of Plant Biologists
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WHOLE PLANT, ENVIRONMENTAL, AND STRESS PHYSIOLOGY |
Oxidative Stress Causes Ferredoxin-NADP+ Reductase Solubilization from the Thylakoid Membranes in Methyl Viologen-Treated Plants
J. F. Palatnik, E. M. Valle and N. Carrillo
Molecular Biology Division, Programa Multidsciplinario de Biologia Experimental, Facultad Ciencias Bioquimicas y Farmaceuticas, Universidad Nacional de Rosario, Suipacha 531, 2000 Rosario, Argentina
The flavoenzyme ferredoxin-NADP+ reductase (FNR) is a member of the
cellular defense barrier against oxidative damage in Escherichia coli. We
evaluated the responses of chloroplast FNR to methyl viologen, a superoxide
radical propagator, in wheat (Triticum aestivum L.) plants and
chloroplasts. Treatments with the herbicide showed little effect on the
levels of FNR protein or transcripts, indicating that expression of this
reductase is not up-regulated by oxidants in plants. Viologens and
peroxides caused solubilization of active FNR from the thylakoids into the
stroma, converting the enzyme from a membrane-bound NADPH producer to a
soluble NADPH consumer. This response appeared specific for FNR, since
other thylakoid proteins were unaffected by the treatments. The
reductase-binding protein was released together with FNR, suggesting that
it might be the target of oxidative modification. Stromal accumulation of a
functional NADPH reductase in response to oxidative stress is formally
analogous to the induction of FNR synthesis observed in E. coli under
similar conditions. FNR solubilization may be playing a crucial role in
maintaining the NADPH/NADP+ homeostasis of the stressed plastid. The
unchecked accumulation of NADPH might otherwise increase the risks of
oxidative damage through a rise in the Mehler reaction rates and/or the
production of hydroxyl radicals.
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