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J Biol Chem, Vol. 274, Issue 3, 1698-1707, January 15, 1999

The Role of Lipoprotein Processing by Signal Peptidase II in the Gram-positive Eubacterium Bacillus subtilis
SIGNAL PEPTIDASE II IS REQUIRED FOR THE EFFICIENT SECRETION OF -AMYLASE, A NON-LIPOPROTEIN

Harold Tjalsma, Vesa P. Kontinen^¶, Zoltán Prágai^**, Hongyan Wu^¶, Rob Meima, Gerard Venema, Sierd Bron, Matti Sarvas^¶, and Jan Maarten van Dijl^§§

From the  Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN Haren, The Netherlands, the ^¶ Vaccine Development Laboratory, National Public Health Institute, Mannerheimintie 166, SF-00300 Helsinki, Finland, the ^** Department of Microbiology, The Medical School, University of Newcastle upon Tyne, Framlington Place, Newcastle upon Tyne NE2 4HH, United Kingdom, and the ^§§ Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands

Computer-assisted analyses indicate that Bacillus subtilis contains approximately 300 genes for exported proteins with an amino-terminal signal peptide. About 114 of these are lipoproteins, which are retained in the cytoplasmic membrane. We have investigated the importance of lipoprotein processing by signal peptidase II (SPase II) for cellular homeostasis, using cells lacking SPase II. The results show that lipoprotein processing is important for cell viability at low and high temperatures, suggesting that lipoproteins are essential for growth under these conditions. Although certain lipoproteins are required for the development of genetic competence, sporulation, and germination, these developmental processes were not affected in the absence of SPase II. Cells lacking SPase II accumulated lipid-modified precursor and mature-like forms of PrsA, a folding catalyst for secreted proteins. These forms of PrsA seem to have a reduced activity, as the secretion of -amylase was strongly impaired. Unexpectedly, type I signal peptidases, which process secretory preproteins, were not involved in alternative amino-terminal processing of pre-PrsA in the absence of SPase II. In conclusion, processing of lipoproteins by SPase II in B. subtilis is not strictly required for lipoprotein function, which is surprising as lipoproteins and type II SPases seem to be conserved in all eubacteria.

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