Osmotin, a plant antifungal protein, subverts signal transduction to enhance fungal cell susceptibility.

11 pages, 2 tablas, 7 figures, 70 references. We are deeply indebted to Henrik Dohlman, Malcolm Whiteway, Michael Gustin, Kunihiro Matsumoto, Ekkehard Leberer, Gerald Fink, and Beverly Errede for providing plasmids; Bradley R. Cairns for STE7 antibody; Kendall J. Blumer for yeast strains; and Jean Clithero for technical assistance.

The plant pathogenesis-related protein osmotin is an antifungal cytotoxic agent that causes rapid cell death in the yeast S. cerevisiae. We show here that osmotin uses a signal transduction pathway to weaken defensive cell wall barriers and increase its cytotoxic efficacy. The pathway activated by osmotin includes the regulatory elements of the mating pheromone response STE4, STE18, STE20, STE5, STE11, STE7, FUS3, KSS1, and STE12. Neither the pheromone receptor nor its associated G protein α subunit GPA1 are required for osmotin action. However, mutation of SST2, a negative regulator of Gα proteins, resulted in supersensitivity to osmotin. Phosphorylation of STE7 was rapidly stimulated by osmotin preceding any changes in cell vitality or morphology. These results demonstrate that osmotin subverts target cell signal transduction as part of its mechanism of action.

This work was supported by grants from the USDA Cooperative Research Program and Purdue Agriculture Experiment Station. This is journal paper number 15,555 of the Purdue University Agricultural Experiment Station.

Peer reviewed