論文

査読有り
2017年6月

Involvement of a conserved GFG motif region in substrate binding by RseP, an Escherichia coli S2P protease

MOLECULAR MICROBIOLOGY
  • Koichiro Akiyama
  • ,
  • Yohei Hizukuri
  • ,
  • Yoshinori Akiyama

104
5
開始ページ
737
終了ページ
751
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1111/mmi.13659
出版者・発行元
WILEY

RseP, an Escherichia coli S2P family intramembrane cleaving protease, is involved in regulation of the extracytoplasmic stress response and membrane quality control through specific cleavage of substrates. Recent research suggested that the PDZ domains and the MRE beta-loop (membrane-reentrant beta-loop) are involved in substrate discrimination; the former would serve to prevent cleavage of substrates with a large periplasmic domain, whereas the latter would directly interact with the substrate's transmembrane segment and induce its conformational change. However, the mechanisms underlying specific substrate recognition and cleavage by RseP are not fully understood. Here, the roles of the N-terminal part of the first cytoplasmic loop region (C1N) of RseP that contains a highly conserved GFG motif were investigated. A Cys modifiability assay suggested that C1N is partly membrane-inserted like the MRE beta-loop. Pro, but not Cys, substitutions in the GFG motif region compromised the proteolytic function of RseP, suggesting the importance of a higher order structure of this motif region. Several lines of evidence indicated that the GFG motif region directly interacts with the substrate and also aids the function of the MRE beta-loop that participates in substrate recognition by RseP. These findings provide insights into the substrate recognition mechanisms of S2P proteases.

Web of Science ® 被引用回数 : 8

リンク情報
DOI
https://doi.org/10.1111/mmi.13659
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/28256773
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000402864900004&DestApp=WOS_CPL
ID情報
  • DOI : 10.1111/mmi.13659
  • ISSN : 0950-382X
  • eISSN : 1365-2958
  • PubMed ID : 28256773
  • Web of Science ID : WOS:000402864900004

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