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THE PLANT CELL, Vol 7, Issue 6 677-688, Copyright © 1995 by American Society of Plant Biologists
Processing and Secretion of a Virally Encoded Antifungal Toxin in Transgenic Tobacco Plants: Evidence for a Kex2p Pathway in Plants
H. Kinal, C. M. Park, J. O. Berry, Y. Koltin and J. A. Bruenn
Department of Biological Sciences, State University of New York at Buffalo, Buffalo, New York 14260
Ustilago maydis is a fungal pathogen of maize. Some strains of U. maydis
encode secreted polypeptide toxins capable of killing other susceptible
strains of U. maydis. We show here that one of these toxins, the KP6 killer
toxin, is synthesized by transgenic tobacco plants containing the viral
toxin cDNA under the control of a cauliflower mosaic virus promoter. The
two components of the KP6 toxin, designated [alpha] and [beta], with
activity and specificity identical to those found in toxin secreted by U.
maydis cells, were isolated from the intercellular fluid of the transgenic
tobacco plants. The [beta] polypeptide from tobacco was identical in size
and N-terminal sequence to the U. maydis KP6 [beta] polypeptide. Processing
of the KP6 preprotoxin in U. maydis requires a subtilisin-like processing
protease, Kex2p, which is present in both animal and fungal cells and is
required for processing of (among other things) small secreted polypeptide
hormones and secreted toxins. Our findings present evidence for Kex2p-like
processing activity in plants. The systemic production of this viral killer
toxin in crop plants may provide a new method of engineering biological
control of fungal pathogens in crop plants.
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