BofA protein inhibits intramembrane proteolysis of pro-sigmaK in an intercompartmental signaling pathway during Bacillus subtilis sporulation.

ABSTRACT: Bacillus subtilis is a bacterium that undergoes a developmental program of sporulation in response to starvation. At the core of the program are sigma factors, whose regulated spatiotemporal activation controls much of the gene expression. Activation of pro-sigma(K) in the mother cell compartment involves regulated intramembrane proteolysis (RIP) in response to a signal from the forespore. RIP is a poorly understood process that is conserved in prokaryotes and eukaryotes. Here, we report a powerful system for studying RIP of pro-sigma(K). Escherichia coli was engineered to coexpress the putative membrane-embedded metalloprotease SpoIVFB with pro-sigma(K) and potential inhibitors of RIP. Overproduction of SpoIVFB and pro-sigma(K) in E. coli allowed accurate and abundant proteolytic processi

SUBMITTER: Zhou R 

PROVIDER: S-EPMC404054 | biostudies-literature | 2004 Apr

REPOSITORIES: biostudies-literature