Roles of the membrane-reentrant β-hairpin-like loop of RseP protease in selective substrate cleavage.

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

SUBMITTER: Akiyama K 

PROVIDER: S-EPMC4597795 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature