Abstract
Proteolysis is a fundamental process used by all forms of life to maintain homeostasis, as well as to remodel the proteome following environmental changes. Here, we explore recent advances in understanding the role of proteolysis during the heat shock response of Escherichia coli. Proteolysis both regulates and contributes directly to and the heat shock response at multiple different levels, from adjusting the levels of the master heat shock response regulator (σ(32)), to eliminating damaged cellular proteins, to altering the activity of chaperones that refold heat-denatured proteins. Recent results illustrate the complexity of the heat shock response and the pervasive role that proteolysis plays in both the cellular response to heat shock and the subsequent limiting of the response, as cells return to a more 'normal' physiological state.