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THE PLANT CELL, Vol 9, Issue 10 1825-1841, Copyright © 1997 by American Society of Plant Biologists
Glucose and Stress Independently Regulate Source and Sink Metabolism and Defense Mechanisms via Signal Transduction Pathways Involving Protein Phosphorylation
R. Ehness, M. Ecker, D. E. Godt and T. Roitsch
Lehrstuhl fur Zellbiologie und Pflanzenphysiologie, Universitat Regensburg, Universitatsstrasse 31, D-93053 Regensburg, Germany
In higher plants, sugars are required not only to sustain heterotrophic
growth but also to regulate the expression of a variety of genes.
Environmental stresses, such as pathogen infection and wounding, activate a
cascade of defense responses and may also affect carbohydrate metabolism.
In this study, the relationship between sugar- and stress-activated signal
transduction pathways and the underlying regulatory mechanism was analyzed.
Photoautotrophically growing suspension culture cells of Chenopodium rubrum
were used as a model system to study the effects of the metabolic regulator
D-glucose and of different stress-related stimuli on photosynthesis, sink
metabolism, and defense response by analyzing the regulation of mRNAs for
representative enzymes of these pathways. Glucose as well as the fungal
elicitor chitosan, the phosphatase inhibitor endothall, and benzoic acid
were shown to result in a coordinated regulatory mechanism. The mRNAs for
phenylalanine ammonia-lyase, a key enzyme of defense response, and for the
sink-specific extracellular invertase were induced. In contrast, the mRNA
for the Calvin cycle enzyme ribulose bisphosphate carboxylase was
repressed. This inverse regulatory pattern was also observed in experiments
with wounded leaves of C. rubrum plants. The differential effect of the
protein kinase inhibitor staurosporine on mRNA regulation demonstrates that
the carbohydrate signal and the stress-related stimuli independently
activate different intracellular signaling pathways that ultimately are
integrated to coordinately regulate source and sink metabolism and activate
defense responses. The various stimuli triggered the transient and rapid
activation of protein kinases that phosphorylate the myelin basic protein.
The involvement of phosphorylation in signal transduction is further
supported by the effect of the protein kinase inhibitor staurosporine on
mRNA levels.
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