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Originally published In Press as doi:10.1074/jbc.M102099200 on April 17, 2001

J. Biol. Chem., Vol. 276, Issue 27, 25230-25235, July 6, 2001
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Distinction between Major and Minor Bacillus Signal Peptidases Based on Phylogenetic and Structural Criteria*

Maarten L. van RoosmalenDagger §, Jan D. H. JongbloedDagger §, Jean-Yves F. Dubois, Gerard VenemaDagger , Sierd BronDagger , and Jan Maarten van Dijl||

From the Dagger  Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands, and the  Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands

The processing of secretory preproteins by signal peptidases (SPases) is essential for cell viability. As previously shown for Bacillus subtilis, only certain SPases of organisms containing multiple paralogous SPases are essential. This allows a distinction between SPases that are of major and minor importance for cell viability. Notably, the functional difference between major and minor SPases is not reflected clearly in sequence alignments. Here, we have successfully used molecular phylogeny to predict major and minor SPases. The results were verified with SPases from various bacilli. As predicted, the latter enzymes behaved as major or minor SPases when expressed in B. subtilis. Strikingly, molecular modeling indicated that the active site geometry is not a critical parameter for the classification of major and minor Bacillus SPases. Even though the substrate binding site of the minor SPase SipV is smaller than that of other known SPases, SipV could be converted into a major SPase without changing this site. Instead, replacement of amino-terminal residues of SipV with corresponding residues of the major SPase SipS was sufficient for conversion of SipV into a major SPase. This suggests that differences between major and minor SPases are based on activities other than substrate cleavage site selection.


* This work was supported by the Dutch Ministry of Economic Affairs through Associatie Biologische Onderzoeksscholen Nederland (to M. L. v.R.), Stichting Levenswetenschappen Grant 805-33.605 (to J. D. H. J), and European Union Grants QLK3-CT-1999-00413 and QLK3-CT-1999-00917 (to S. B, J. D. H. J., J. Y. D., and J. M. v.D.).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.

§ Both authors contributed equally to this work.

|| To whom correspondence should be addressed. Tel.: 31-50-363-3079; Fax: 31-50-363-2348; E-mail: J.M.VAN.DIJL@FARM.RUG.NL.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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