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THE PLANT CELL, Vol 1, Issue 4 447-457, Copyright © 1989 by American Society of Plant Biologists
Functional Implications of the Subcellular Localization of Ethylene-Induced Chitinase and [beta]-1,3-Glucanase in Bean Leaves
F. Mauch and L. A. Staehelin
Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347
Plants respond to an attack by potentially pathogenic organisms and to the
plant stress hormone ethylene with an increased synthesis of hydrolases
such as chitinase and [beta]-1,3-glucanase. We have studied the subcellular
localization of these two enzymes in ethylene-treated bean leaves by
immunogold cytochemistry and by biochemical fractionation techniques. Our
micrographs indicate that chitinase and [beta]-1,3-glucanase accumulate in
the vacuole of ethylene-treated leaf cells. Within the vacuole label was
found predominantly over ethylene-induced electron dense protein
aggregates. A second, minor site of accumulation of [beta]-1,3-glucanase
was the cell wall, where label was present nearly exclusively over the
middle lamella surrounding intercellular air spaces. Both kinds of
antibodies labeled Golgi cisternae of ethylene-treated tissue, suggesting
that the newly synthesized chitinase and [beta]-1,3-glucanase are processed
in the Golgi apparatus. Biochemical fractionation studies confirmed the
accumulation in high concentrations of both chitinase and
[beta]-1,3-glucanase in isolated vacuoles, and demonstrated that only
[beta]-1,3-glucanase, but not chitinase, was present in intercellular
washing fluids collected from ethylene-treated leaves. Based on these
results and earlier studies, we propose a model in which the
vacuole-localized chitinase and [beta]-1,3-glucanase are used as a last
line of defense to be released when the attacked host cells lyse. The cell
wall-localized [beta]-1,3-glucanase, on the other hand, would be involved
in recognition processes, releasing defense activating signaling molecules
from the walls of invading pathogens.
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