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Background  The microbial cell factory  Bacillus subtilis  is a popular industrial platform for high-level production of secreted technical enzymes. Nonetheless, the effective secretion of particular heterologous enzymes remains challenging. Over the past decades various studies have tackled this problem, and major improvements were achieved by optimizing signal peptides or removing proteases involved in product degradation. On the other hand, serious bottlenecks in the protein export process per se remained enigmatic, especially for protein secretion at commercially significant levels by cells grown to high density. The aim of our present study was to assess the relevance of the intramembrane protease RasP for high-level protein production in  B. subtilis .    Results  Deletion of the  rasP  gene resulted in reduced precursor processing and extracellular levels of the overproduced α-amylases AmyE from  B. subtilis  and AmyL from  Bacillus licheniformis . Further, secretion of the overproduced serine protease BPN’ from  Bacillus amyloliquefaciens  was severely impaired in the absence of RasP. Importantly, overexpression of  rasP  resulted in threefold increased production of a serine protease from  Bacillus clausii , and 2.5- to 10-fold increased production of an AmyAc α-amylase from  Paenibacillus curdlanolyticus , depending on the culture conditions. Of note, growth defects due to overproduction of the two latter enzymes were suppressed by  rasP -overexpression.    Conclusion  Here we show that an intramembrane protease, RasP, sets a limit to high-level production of two secreted heterologous enzymes that are difficult to produce in the  B. subtilis  cell factory. This finding was unexpected and suggests that proteolytic membrane sanitation is key to effective enzyme production in  Bacillus .

Intramembrane protease RasP boosts protein production in Bacillus