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Starvation yields a drastic decrease in outer-membrane permeability to a periplasmic foreign protein in Myxococcus
K Laval-Favre1, B Letouvet-Pawlak, S Barray
1Equipe de Génétique Bactérienne, URA 203 CNRS, Faculté des Sciences de Rouen, Mont-Saint-Aignan, France.
Microbiology (Reading, England)
|December 1, 1995
Summary
Starvation halts the secretion of periplasmic proteins in Myxococcus xanthus during development. This protein secretion change during development may utilize a different pathway than in vegetative cells.
Area of Science:
- Microbiology
- Molecular Biology
- Bacterial Physiology
Background:
- Myxococcus xanthus is a model organism for studying bacterial development.
- Recombinant strains can be engineered to study protein production and secretion.
- Previously, AppA protein was shown to be secreted into the medium by vegetative M. xanthus cells.
Purpose of the Study:
- To investigate the secretion of periplasmic proteins in M. xanthus during starvation-induced development.
- To determine if starvation conditions affect protein secretion pathways.
- To compare protein secretion in vegetative versus developing cells.
Main Methods:
- Construction of a recombinant M. xanthus strain producing E. coli beta-galactosidase and AppA protein.
- Culturing M. xanthus under vegetative and starvation conditions.
- Monitoring AppA protein accumulation in the periplasm and release into the medium over time.
Main Results:
- Periplasmic AppA protein release into the medium was significantly reduced during 20 hours of starvation-induced development.
- This lack of secretion was attributed to starvation itself, not the arrest of foreign protein synthesis.
- The ability of cells to undergo development was not required for the observed lack of secretion.
Conclusions:
- Starvation conditions alter protein secretion pathways in M. xanthus.
- Protein secretion during early starvation-induced development may differ from vegetative secretion.
- This suggests distinct mechanisms for protein export under different cellular conditions.