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THE PLANT CELL, Vol 2, Issue 1 7-18, Copyright © 1990 by American Society of Plant Biologists
Peroxidase-Induced Wilting in Transgenic Tobacco Plants
L. M. Lagrimini, S. Bradford and S. Rothstein
Department of Horticulture and Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210-1096
Peroxidases are a family of isoenzymes found in all higher plants. However,
little is known concerning their role in growth, development, or response
to stress. Plant peroxidases are heme-containing monomeric glycoproteins
that utilize either H2O2 or O2 to oxidize a wide variety of molecules. To
obtain more information on possible in planta functions of peroxidases, we
have used a cDNA clone for the primary isoenzyme form of peroxidase to
synthesize high levels of this enzyme in transgenic plants. We were able to
obtain Nicotiana tabacum and N. sylvestris transformed plants with
peroxidase activity that is 10-fold higher than in wild-type plants by
introducing a chimeric gene composed of the cauliflower mosaic virus 35S
promoter and the tobacco anionic peroxidase cDNA. The elevated peroxidase
activity was a result of increased levels of two anionic peroxidases in N.
tabacum, which apparently differ in post-translational modification.
Transformed plants of both species have the unique phenotype of chronic
severe wilting through loss of turgor in leaves, which was initiated at the
time of flowering. The peroxidase-induced wilting was shown not to be an
effect of diminished water uptake through the roots, decreased conductance
of water through the xylem, or increased water loss through the leaf
surface or stomata. Possible explanations for the loss of turgor, and the
significance of these types of experiments in studying isoenzyme families,
are discussed.
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