A PDZ Switch for a Cellular Stress Response
نویسندگان
چکیده
The accumulation of misfolded porins in the periplasm of bacteria triggers a proteolytic cascade, initiated by activation of DegS, a member of the family of HtrA proteases. Activation of DegS ultimately leads to the expression of genes encoding the periplasmic protein folding machinery. A new study now reveals that binding of exposed C-termini of unassembled porins to the PDZ domain of DegS induces structural rearrangements that activate the catalytic site of the protease domain.
منابع مشابه
Allosteric Activation of DegS, a Stress Sensor PDZ Protease
Regulated intramembrane proteolysis is a method for transducing signals between cellular compartments. When protein folding is compromised in the periplasm of E. coli, the C termini of outer-membrane proteins (OMPs) bind to the PDZ domains of the trimeric DegS protease and activate cleavage of RseA, a transmembrane transcriptional regulator. We show here that DegS is an allosteric enzyme. OMP b...
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عنوان ژورنال:
- Cell
دوره 117 شماره
صفحات -
تاریخ انتشار 2004