The Escherichia coli sigma(super.E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor

Article Abstract:

The Escherichia coli sigma(super.E)-dependent extracytoplasmic stress response is discussed. The response is controlled by the regulated proteolysis of an anti-sigma factor. The sigma(super.E) activity is determined largely by the ratio of RseA to sigma(super.E). RseA degrades quickly responding to extracytoplasmic stress. That leads to an increase in the free pool of sigma(super.E) and the stress response is set up.

United States, Statistical Data Included, Physiological aspects, Stress (Physiology), Heat shock proteins, Cytochemistry, Proteolysis, Cell physiology, Cell compartmentation

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A chaperone network controls the heat shock response in E.coli

Article Abstract:

The role of the two chaperones, GroEL/S and HtpG, in regulation of the heat shock response in Escherichia coli is investigated. In vivo and in vitro evidence supporting the idea that GroEL/S, but HtpG, is used to sense the protein folding state of the cell is presented and it is further shown that GroEL/S is used together with the DnaK chaperone machine to regulate heat shock gene transcription.

Molecular chaperones

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Regulon and promoter analysis of the E. coli heat-shock factor, [sigma.sup.32], reveals a multifaceted cellular response to heat stress

Article Abstract:

Genome-wide expression analysis and promoter validation to identify genes directly regulated by [sigma.sup.32] is used. The number of genes validated to be transcribed by [sigma.sup.32] is tripled and new sights into the cellular role of this response is provided.

Gene expression, Genetic research

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