Allosteric Activation of a Bacterial Stress Sensor
نویسندگان
چکیده
In Gram-negative bacteria, envelope stress signals such as unfolded outer membrane proteins (OMP) activate the periplasmic protease DegS. This protease then triggers a cellular pathway to alleviate the stress. Now Sohn et al. (2007) show conclusively that inhibition of DegS is relieved allosterically by binding of the C-terminal sequences in unfolded OMPs to the PDZ domain of DegS.
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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ورودعنوان ژورنال:
- Cell
دوره 131 شماره
صفحات -
تاریخ انتشار 2007