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Title: Roles of the membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavage.
Authors: Akiyama, Koichiro
Mizuno, Shinya
Hizukuri, Yohei  kyouindb  KAKEN_id
Mori, Hiroyuki  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-0429-1269 (unconfirmed)
Nogi, Terukazu
Akiyama, Yoshinori  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0003-4483-5408 (unconfirmed)
Author's alias: 秋山, 芳展
Issue Date: 8-Oct-2015
Publisher: eLife Sciences Publications Ltd.
Journal title: eLife
Volume: 4
Thesis number: e08928
Abstract: Molecular mechanisms underlying substrate recognition and cleavage by Escherichia coli RseP, which belongs to S2P family of intramembrane-cleaving proteases, remain unclear. We examined the function of a conserved region looped into the membrane domain of RseP to form a β-hairpin-like structure near its active site in substrate recognition and cleavage. We observed that mutations disturbing the possible β-strand conformation of the loop impaired RseP proteolytic activity and that some of these mutations resulted in the differential cleavage of different substrates. Co-immunoprecipitation and crosslinking experiments suggest that the loop directly interacts with the transmembrane segments of substrates. Helix-destabilising mutations in the transmembrane segments of substrates suppressed the effect of loop mutations in an allele-specific manner. These results suggest that the loop promotes substrate cleavage by selectively recognising the transmembrane segments of substrates in an extended conformation and by presenting them to the proteolytic active site, which contributes to substrate discrimination.
Rights: This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. (http://creativecommons.org/licenses/by/4.0/)
URI: http://hdl.handle.net/2433/207637
DOI(Published Version): 10.7554/eLife.08928
PubMed ID: 26447507
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