Bacillus subtilis Intramembrane Protease RasP Activity in Escherichia coli and In Vitro.

ABSTRACT: RasP is a predicted intramembrane metalloprotease of Bacillus subtilis that has been proposed to cleave the stress response anti-sigma factors RsiW and RsiV, the cell division protein FtsL, and remnant signal peptides within their transmembrane segments. To provide evidence for direct effects of RasP on putative substrates, we developed a heterologous coexpression system. Since expression of catalytically inactive RasP E21A inhibited expression of other membrane proteins in Escherichia coli, we added extra transmembrane segments to RasP E21A, which allowed accumulation of most other membrane proteins. A corresponding active version of RasP appeared to promiscuously cleave coexpressed membrane proteins, except those with a large periplasmic domain. However, stable cleavage pro

SUBMITTER: Parrell D 

PROVIDER: S-EPMC5585704 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature