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A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli

A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli

Journal of Biological Chemistry 283(50): 35042-35052

The sigma(E) pathway of extracytoplasmic stress responses in Escherichia coli is activated through sequential cleavages of the anti-sigma(E) protein, RseA, by membrane proteases DegS and RseP. Without the first cleavage by DegS, RseP is unable to cleave full-length RseA. We previously showed that a PDZ-like domain in the RseP periplasmic region is essential for this negative regulation of RseP. We now isolated additional deregulated RseP mutants. Many of the mutations affected a periplasmic region that is N-terminal to the previously defined PDZ domain. We expressed these regions and determined their crystal structures. Consistent with a recent prediction, our results indicate that RseP has tandem, circularly permutated PDZ domains (PDZ-N and PDZ-C). Strikingly, almost all the strong mutations have been mapped around the ligand binding cleft region in PDZ-N. These results together with those of an in vitro reaction reproducing the two-step RseA cleavage suggest that the proteolytic function of RseP is controlled by ligand binding to PDZ-N.

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Accession: 051203984

Download citation: RISBibTeXText

PMID: 18945679

DOI: 10.1074/jbc.M806603200

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