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

研究成果: Article査読

36 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)35042-35052
ページ数11
ジャーナルJournal of Biological Chemistry
283
50
DOI
出版ステータスPublished - 2008 12月 12
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

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