Heat Shock (sigma32 and HrcA/CIRCE) Regulons in Beta-, Gamma- And Epsilon-Proteobacteria

J Mol Microbiol Biotechnol. 2003;6(3-4):174-81. doi: 10.1159/000077248.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Betaproteobacteria / genetics*
  • Betaproteobacteria / physiology
  • DNA-Binding Proteins
  • Endopeptidases / genetics
  • Endopeptidases / metabolism
  • Epsilonproteobacteria / genetics*
  • Epsilonproteobacteria / physiology
  • Feedback, Physiological
  • Gammaproteobacteria / genetics*
  • Gammaproteobacteria / physiology
  • Genes, Bacterial
  • Heat-Shock Proteins / genetics*
  • Heat-Shock Proteins / metabolism
  • Heat-Shock Response
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Operon
  • Regulon*
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism
  • Sigma Factor / genetics*
  • Sigma Factor / metabolism

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Repressor Proteins
  • Sigma Factor
  • heat-shock sigma factor 32
  • Endopeptidases