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The Bacillus subtilis ABC transporter EcsAB influences intramembrane proteolysis through RasP

¹ Institute of Genetics, University of Bayreuth, Bayreuth, Germany
² Infection Pathogenesis Laboratory, Department of Viral Diseases and Immunology, National Public Health Institute, Helsinki, Finland

Correspondence
Thomas Wiegert
thomas.wiegert{at}uni-bayreuth.de

The Bacillus subtilis ^W regulon is induced by different stresses that most probably affect integrity of the cell envelope. The activity of the extracytoplasmic function (ECF) sigma factor ^W is modulated by the transmembrane anti-sigma factor RsiW, which undergoes stress-induced degradation in a process known as regulated intramembrane proteolysis, finally resulting in the release of ^W and the transcription of ^W-controlled genes. Mutations in the ecsA gene, which encodes an ATP binding cassette (ABC) of an ABC transporter of unknown function, block site-2 proteolysis of RsiW by the intramembrane cleaving protease RasP (YluC). In addition, degradation of the cell division protein FtsL, which represents a second RasP substrate, is blocked in an ecsA-negative strain. The defect in ^W induction of an ecsA-knockout strain could be partly suppressed by overproducing RasP. A B. subtilis rasP-knockout strain displayed the same pleiotropic phenotype as an ecsA knockout, namely defects in processing -amylase, in competence development, and in formation of multicellular structures known as biofilms.