Publication | Open Access
Model for Stress-induced Protein Degradation in <i>Lemna minor</i>
29
Citations
20
References
1980
Year
Lemna Minor FrondsMolecular BiologyCellular PhysiologyOxidative StressStressProtein FoldingProteomicsProtein DegradationProtein ChemistryProtein Quality ControlProtein FunctionOsmotic StressBiochemistryProtein TransportProtein BiosynthesisReductive StressNatural SciencesCellular BiochemistryMedicineStress-induced Protein Degradation
Transfer of Lemna minor fronds to adverse or stress conditions produces a large increase in the rate of protein degradation. Cycloheximide partially inhibits stress-induced protein degradation and also partially inhibits the protein degradation which occurs in the absence of stress. The increased protein degradation does not appear to be due to an increase in activity of soluble proteolytic enzymes. Biochemical evidence indicates that stress, perhaps acting via hormones, affects the permeability of certain membranes, particularly the tonoplast. A general model for stress-induced protein degradation is presented in which changes in membrane properties allow vacuolar proteolytic enzymes increased access to cytoplasmic proteins.
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