title: Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response.
abstract: The heat shock response (HSR) is a homeostatic response that maintains the proper protein-folding environment in the cell. This response is universal, and many of its components are well conserved from bacteria to humans. In this review, we focus on the regulation of one of the most well-characterized HSRs, that of Escherichia coli. We show that even for this simple model organism, we still do not fully understand the central component of heat shock regulation, a chaperone-mediated negative feedback loop. In addition, we review other components that contribute to the regulation of the HSR in E. coli and discuss how these additional components contribute to regulation. Finally, we discuss recent genomic experiments that reveal additional functional aspects of the HSR.
authors.affiliation: Department of Biochemistry, University of California at San Francisco, San Francisco, CA 94158-2517, USA.
authors.forename: Eric
authors.initials: E
authors.lastname: Guisbert
authors.forename: Takashi
authors.initials: T
authors.lastname: Yura
authors.forename: Virgil A
authors.initials: VA
authors.lastname: Rhodius
authors.forename: Carol A
authors.initials: CA
authors.lastname: Gross
mesh_terms: D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006360:Heat-Shock Proteins; D018869:Heat-Shock Response / Q000235:genetics / Q000502:physiology; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D012808:Sigma Factor / Q000235:genetics / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D012808:Sigma Factor; C069774:heat-shock sigma factor 32
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