Revival of the Escherichia coli heat shock response after two decades with a small Hsp in a critical but distinct act.

Abstract

The heat stress response is an essential defense mechanism in all organisms. Heat shock proteins (Hsps) are produced in response to thermal stress, with their expression levels regulated by heat shock transcription factors. In Escherichia coli, the key transcription factor σ³² positively regulates Hsp expression. Studies from over two decades ago revealed that σ³² abundance is negatively controlled under normal conditions, mainly through degradation mechanisms involving DnaK, GroEL, and FtsH. Beyond this established mechanism, recent findings indicate that a small heat shock protein IbpA also plays a role in the translational regulation of σ³², adding a new layer to the established model. This review highlights the role of a new actor, IbpA, which strongly suppresses σ³² expression under non-stress conditions and markedly increases it during heat shock.