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Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis

Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA

Evidence is presented that the activation of the RNA polymerase factor ^W in Bacillus subtilis by regulated intramembrane proteolysis is governed by a novel, membrane-embedded protease. The ^W factor is activated by proteolytic destruction of the membrane-bound anti-^W factor RsiW in response to antimicrobial peptides and other agents that damage the cell envelope. RsiW is destroyed by successive proteolytic events known as Site-1 and Site-2 cleavage. Site-2 cleavage is mediated by a member of the SpoIVFB-S2P family of intramembrane-acting metalloproteases, but the protease responsible for Site-1 cleavage was unknown. We have identified a previously uncharacterized, multipass membrane protein called PrsW (annotated YpdC) that is both necessary and sufficient (when artificially produced in an unrelated host bacterium) for Site-1 cleavage of RsiW. PrsW is a member of a widespread family of membrane proteins that includes at least one previously known protease. We identify residues important for proteolysis and a cluster of acidic residues involved in sensing antimicrobial peptides and cell envelope stress.

[Keywords: Signal transduction; Site-1 cleavage; ECF factor; antimicrobial peptides]

Received April 14, 2006; revised version accepted May 30, 2006.

E-MAIL losick{at}mcb.harvard.edu; FAX (617) 496-4642.

Supplemental material is available at http://www.genesdev.org.

Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.1440606

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