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

Kenji Inaba, Mamoru Suzuki, Ken Ichi Maegawa, Shuji Akiyama, Koreaki Ito, Yoshinori Akiyama

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

The σE pathway of extracytoplasmic stress responses in Escherichia coli is activated through sequential cleavages of the anti-σE 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.

Original languageEnglish
Pages (from-to)35042-35052
Number of pages11
JournalJournal of Biological Chemistry
Volume283
Issue number50
DOIs
Publication statusPublished - 2008 Dec 12
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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