Heat Shock (σ32 and HrcA/CIRCE) Regulons in β-, γ- and ε-Proteobacteria

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Abstract
During heat shock, the main strategy of an organism is defense from denatured proteins. This is performed by chaperones that refold and proteases that cut abnormal proteins. In studying the sigma(32) and HrcA regulons in beta- and gamma-proteobacteria, we have found some new potential participants in the heat shock response and proposed the protein disulfide isomerase function for one of them. We describe the connection between the two regulons through cross-regulation of the HrcA repressor and sigma(32) in some beta-proteobacteria. Finally, we predict the binding signal for HrcA in epsilon-proteobacteria.

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