Determinants of regulated proteolysis in signal transduction

Article Abstract:

The main players of the [sigma.sup.E] signal transduction cascade are identified and the mechanism of signal sensing and proteolytic activation of the rate-limiting factor DegS is explained at the atomic level. It is found that the complete process from signal sensing to [sigma.sup.E] release takes less than 2 minute allowing a rapid response to protein folding or mislocalization problems in the cell envelope.

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Regulation of the [sigma]E stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress

Article Abstract:

A study observed how the PDZ domain kept the protease inactive in a resting state that is required for the functioning of the [sigma]E stress response. The results noted that the PDZ domain and L2 of DegS define a novel molecular switch allowing strict regulation of the [sigma]E stress response system.

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Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease

Article Abstract:

The crystal structures of three distinct states of DegS from E.coli are presented. The structural data illustrates that DegS acts as a periplasmic stress sensor and a novel regulatory role for PDZ domains and unevil a novel mechanism of reversible protease activation is suggested.

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