Robustness analysis of the heat shock response in E. coli

Abstract

The bacterial heat shock response refers to the mechanism by which bacteria react to a sudden increase in the ambient temperature of growth. The consequences of such an unmediated temperature increase at the cellular level is the unfolding, misfolding, or aggregation of cell proteins, which threatens the life of the cell. Cells respond to the heat stress by initiating the production of heat-shock proteins whose function is to refold denatured proteins into their native states. The heat shock response, through the elevated synthesis of molecular chaperones and proteases, enables the repair of protein damage and the degradation of aggregated proteins. In a previous work (Kurata et al., 2001), we have devised a dynamic model for the heat shock response in E. coli. In the present paper, we provide a thorough discussion of the dynamical nature of this model. We use sensitivity analysis and simulation tools to illustrate the remarkable efficiency, robustness, and stability of the heat shock response system.