論文

査読有り
2017年

Biochemical Characterization of Function and Structure of RseP, an Escherichia coli S2P Protease

ENZYMOLOGY AT THE MEMBRANE INTERFACE: INTRAMEMBRANE PROTEASES
  • Y. Hizukuri
  • ,
  • K. Akiyama
  • ,
  • Y. Akiyama

584
開始ページ
1
終了ページ
33
記述言語
英語
掲載種別
論文集(書籍)内論文
DOI
10.1016/bs.mie.2016.09.044
出版者・発行元
ELSEVIER ACADEMIC PRESS INC

Intramembrane-cleaving proteases (I-CLiPs) are a group of membrane-associated proteases with a unique feature: they are believed to cleave their substrate within the hydrophobic lipid bilayer, even though peptide bond hydrolysis requires a water molecule. Escherichia coli RseP, which belongs to the S2P zinc metalloprotease family of I-CLiPs, plays an essential role in activation of a cell envelope stress response through cleavage of anti-sE protein RseA, a single-span transmembrane protein. A recent study showed that it also cleaves remnant signal peptides generated upon membrane translocation of secretory proteins. Here, we describe several methods for characterization of the proteolytic functions and structure of RseP mainly in vivo, including a proteolytic activity assay using model substrates, an in vitro analysis of cleavage of signal peptides in a detergent solution and in the membrane vesicles, structural analysis of membrane-embedded RseP based on the thiol modifiability of introduced cysteine residues, and the protein interaction analysis by in vivo cross-linking protocols.

Web of Science ® 被引用回数 : 4

リンク情報
DOI
https://doi.org/10.1016/bs.mie.2016.09.044
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/28065260
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000403271000002&DestApp=WOS_CPL
ID情報
  • DOI : 10.1016/bs.mie.2016.09.044
  • ISSN : 0076-6879
  • PubMed ID : 28065260
  • Web of Science ID : WOS:000403271000002

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