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Originally published In Press as doi:10.1074/jbc.M002676200 on May 24, 2000

J. Biol. Chem., Vol. 275, Issue 33, 25102-25108, August 18, 2000
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Conserved Serine and Histidine Residues Are Critical for Activity of the ER-type Signal Peptidase SipW of Bacillus subtilis*

Harold TjalsmaDagger §, Axel G. Stöver||**, Adam Driks||, Gerard VenemaDagger , Sierd BronDagger Dagger Dagger , and Jan Maarten van DijlDagger Dagger Dagger §§

From the Dagger  Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN Haren, The Netherlands and the  Department of Microbiology and Immunology, Loyola University Medical Center, Maywood, Illinois 60153

Type I signal peptidases (SPases) are required for the removal of signal peptides from translocated proteins and, subsequently, release of the mature protein from the trans side of the membrane. Interestingly, prokaryotic (P-type) and endoplasmic reticular (ER-type) SPases are functionally equivalent, but structurally quite different, forming two distinct SPase families that share only few conserved residues. P-type SPases were, so far, exclusively identified in eubacteria and organelles, whereas ER-type SPases were found in the three kingdoms of life. Strikingly, the presence of ER-type SPases appears to be limited to sporulating Gram-positive eubacteria. The present studies were aimed at the identification of potential active site residues of the ER-type SPase SipW of Bacillus subtilis, which is required for processing of the spore-associated protein TasA. Conserved serine, histidine, and aspartic acid residues are critical for SipW activity, suggesting that the ER-type SPases employ a Ser-His-Asp catalytic triad or, alternatively, a Ser-His catalytic dyad. In contrast, the P-type SPases employ a Ser-Lys catalytic dyad (Paetzel, M., Dalbey, R. E., and Strynadka, N. C. J. (1998) Nature 396, 186-190). Notably, catalytic activity of SipW was not only essential for pre-TasA processing, but also for the incorporation of mature TasA into spores.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by Genencor International (Rijswijk, The Netherlands) and Gist-brocades B.V. (Delft, The Netherlands).

|| Supported by Public Health Service Grant GM539898 from the National Institutes of Health and a grant from the Schweppe Foundation.

** Supported in part by a Schmitt fellowship.

Dagger Dagger Supported by Biotechnology Grants Bio4-CT95-0278 and Bio4-CT96-0097 and "Quality of Life and Management of Living Resources" Grants QLK3-CT-1999-00415 and QLK3-CT-1999-00917 from the European Union.

§§ To whom correspondence should be addressed. Present address: Dept. of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. Tel.: 31-503633079; Fax: 31-503632348; E-mail: j.m.van.dijl@farm.rug.nl.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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