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Effects of recombinant protein misfolding and aggregation on bacterial membranes
- Publication Year :
- 2009
- Publisher :
- Elsevier, 2009.
-
Abstract
- The expression of recombinant proteins is known to induce a metabolic rearrangement in the host cell. We used aggregation-sensitive model systems to study the effects elicited in Escherichia coli cells by the aggregation of recombinant glutathione-S-transferase and its fusion with the green fluorescent protein that, according to the expression conditions, accumulate intracellularly as soluble protein, or soluble and insoluble aggregates. We show that the folding state of the recombinant protein and the complexity of the intracellular aggregates critically affect the cell response. Specifically, protein misfolding and aggregation induce changes in specific host proteins involved in lipid metabolism and oxidative stress, a reduction in the membrane permeability, as well as a rearrangement of its lipid composition. The temporal evolution of the host cell response and that of the aggregation process pointed out that the misfolded protein and soluble aggregates are responsible for the membrane modifications and the changes in the host protein levels. Interestingly, native recombinant protein and large insoluble aggregates do not seem to activate stress markers and membrane rearrangements.
- Subjects :
- Protein Folding
Vesicle-associated membrane protein 8
Cell Membrane Permeability
Recombinant protein
Membrane permeability
Recombinant Fusion Proteins
Membrane lipids
Green Fluorescent Proteins
Biophysics
Protein aggregation
Biology
Biochemistry
Analytical Chemistry
Green fluorescent protein
Cell membrane
Membrane Lipids
Genes, Reporter
Spectroscopy, Fourier Transform Infrared
Escherichia coli
medicine
Molecular Biology
Glutathione Transferase
Cell Membrane
Fourier transform infrared spectroscopy
Membrane lipid
beta-Galactosidase
BIO/10 - BIOCHIMICA
Cell biology
Stress metabolism
Oxidative Stress
medicine.anatomical_structure
Small chaperone
Protein folding
Intracellular
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....82fdee3fbbfcefde94b063f245bb4190