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Applied and Environmental Microbiology, April 2005, p. 1899-1908, Vol. 71, No. 4
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.4.1899-1908.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Genes Involved in SkfA Killing Factor Production Protect a Bacillus subtilis Lipase against Proteolysis

Helga Westers,^1,2, Peter G. Braun,^1, Lidia Westers,¹ Haike Antelmann,³ Michael Hecker,³ Jan D. H. Jongbloed,² Hirofumi Yoshikawa,⁴ Teruo Tanaka,⁵ Jan Maarten van Dijl,^1* and Wim J. Quax¹

Department of Pharmaceutical Biology, University of Groningen, Groningen,¹ Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Haren, The Netherlands,² Institut für Mikrobiologie und Molekularbiologie, Ernst-Moritz-Arndt-Universität Greifswald, Greifswald, Germany,³ Department of Bioscience, Tokyo University of Agriculture, Sakuragaoka, Setagaya-ku, Tokyo,⁴ Department of Marine Science, School of Marine Science and Technology, Tokai University, Shimizuorido, Shizuoka, Japan⁵

Received 13 May 2004/ Accepted 11 November 2004

Small lipases of Bacillus species, such as LipA from Bacillus subtilis, have a high potential for industrial applications. Recent studies showed that deletion of six AT-rich islands from the B. subtilis genome results in reduced amounts of extracellular LipA. Here we demonstrate that the reduced LipA levels are due to the absence of four genes, skfABCD, located in the prophage 1 region. Intact skfABCD genes are required not only for LipA production at wild-type levels by B. subtilis 168 but also under conditions of LipA overproduction. Notably, SkfA has bactericidal activity and, probably, requires the SkfB to SkfD proteins for its production. The present results show that LipA is more prone to proteolytic degradation in the absence of SkfA and that high-level LipA production can be improved significantly by employing multiple protease-deficient B. subtilis strains. In conclusion, our findings imply that SkfA protects LipA, directly or indirectly, against proteolytic degradation. Conceivably, SkfA could act as a modulator in LipA folding or as a protease inhibitor.

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* Corresponding author. Present address: Department of Molecular Bacteriology, University of Groningen, Hanzeplein 1, P.O. Box 30 001, 9700 RB Groningen, the Netherlands. Phone: (31) 50 363 3079. Fax: (31) 50 363 3528. E-mail: j.m.van.dijl{at}med.rug.nl.

These authors contributed equally to this work.

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Applied and Environmental Microbiology, April 2005, p. 1899-1908, Vol. 71, No. 4
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.4.1899-1908.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

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