Sep 24, 2009

Proteome analysis of the Escherichia coli heat shock response under steady-state conditions

Proteome Science
Svenja LüdersEzequiel Franco-Lara

Abstract

In this study a proteomic approach was used to investigate the steady-state response of Escherichia coli to temperature up-shifts in a cascade of two continuously operated bioreactors. The first reactor served as cell source with optimal settings for microbial growth, while in the second chemostat the cells were exposed to elevated temperatures. By using this reactor configuration, which has not been reported to be used for the study of bacterial stress responses so far, it is possible to study temperature stress under well-defined, steady-state conditions. Specifically the effect on the cellular adaption to temperature stress using two-dimensional gel electrophoresis was examined and compared at the cultivation temperatures of 37 degrees C and 47.5 degrees C. As expected, the steady-state study with the double bioreactor configuration delivered a different protein spectrum compared to that obtained with standard batch experiments in shaking flasks and bioreactors. Setting a high cut-out spot-to-spot size ratio of 5, proteins involved in defence against oxygen stress, functional cell envelope proteins, chaperones and proteins involved in protein biosynthesis, the energy metabolism and the amino acid biosynthesis were found to b...Continue Reading

  • References90
  • Citations22

References

  • References90
  • Citations22

Citations

Mentioned in this Paper

Pathologic Cytolysis
Microorganism
Metabolic Process, Cellular
Buffers
Heat shock proteins
Biochemical Pathway
Biological Adaptation to Stress
LARS gene
Protein Degradation, Regulatory
Hydrogen Peroxide

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