Protein misfolding in the cell envelope of Escherichia coli: new signaling pathways.
Depending on their cellular localization, misfolded proteins in Escherichia coli trigger two different heat-shock responses. Cytoplasmic proteins induce the 'classical' heat-shock regulon transcribed by the E sigma 32 polymerase. By contrast, misfolding of proteins in the cell envelope induces the newly described E sigma E-dependent regulon. This implies that there is an inducible transduction machinery in the inner membrane. The response to protein misfolding in the cell envelope is a finely tuned system regulated by a cascade of phosphorylation and dephosphorylation reactions.
Missiakas
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Centre National de Recherche Scientifique LIDSM, Marseille, France.
Raina
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D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D006358:Hot Temperature; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D015398:Signal Transduction
D001426:Bacterial Proteins; D008565:Membrane Proteins