Stress induced by recombinant protein production in Escherichia coli.
Strong production of recombinant proteins interferes with cellular processes in many ways. Drainage of precursors and energy urges the cell to readjust metabolic fluxes and enzyme composition, stress responses are induced, and hence the cellular activity is shifted from growth to reorganisation of biomass. This may result in inhibition of growth or low level of product accumulation. The extent of the bacterial stress response is determined by the specific properties of the recombinant protein, and by the rates of transcription and translation. Taking into account the capacities of the host for protein processing and physiological adaptation, production schemes can be developed that enhance volumetric productivity and sustainability of the process.
Hoffmann
Frank
F
Institut für Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle, Germany.
Rinas
Ursula
U
D000222:Adaptation, Physiological / Q000502:physiology; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics; D004926:Escherichia coli / Q000502:physiology*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D018869:Heat-Shock Response / Q000502:physiology*; D018384:Oxidative Stress / Q000502:physiology*; D011994:Recombinant Proteins / Q000096:biosynthesis*; D013014:SOS Response, Genetics / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*
D001426:Bacterial Proteins; D011994:Recombinant Proteins