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J Biol Chem, Vol. 274, Issue 35, 24585-24592, August 27, 1999

Signal Peptide Peptidase- and ClpP-like Proteins of Bacillus subtilis Required for Efficient Translocation and Processing of Secretory Proteins

Albert Bolhuisa, Arne Matzend, Hanne-Leena Hyyryläinenf, Vesa P. Kontinenf, Rob Meimaa, Jerome Chapuisi, Gerard Venemaa, Sierd Brona, Roland Freudld, and Jan Maarten van Dijla

From the a Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN Haren, The Netherlands, the d Institut für Biotechnologie 1, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany, the f Laboratory of Vaccine Development, National Public Health Insitute, FIN-00300 Helsinki, Finland, and i INRA, Laboratoire de Génétique Microbienne, Institut National de la Recherche Agronomique, Domain de Vilvert, 78352 Jouy en Josas Cedex, France

Signal peptides direct the export of secretory proteins from the cytoplasm. After processing by signal peptidase, they are degraded in the membrane and cytoplasm. The resulting fragments can have signaling functions. These observations suggest important roles for signal peptide peptidases. The present studies show that the Gram-positive eubacterium Bacillus subtilis contains two genes for proteins, denoted SppA and TepA, with similarity to the signal peptide peptidase A of Escherichia coli. Notably, TepA also shows similarity to ClpP proteases. SppA of B. subtilis was only required for efficient processing of pre-proteins under conditions of hyper-secretion. In contrast, TepA depletion had a strong effect on pre-protein translocation across the membrane and subsequent processing, not only under conditions of hyper-secretion. Unlike SppA, which is a typical membrane protein, TepA appears to have a cytosolic localization, which is consistent with the observation that TepA is involved in early stages of the secretion process. Our observations demonstrate that SppA and TepA have a role in protein secretion in B. subtilis. Based on their similarity to known proteases, it seems likely that SppA and TepA are specifically required for the degradation of proteins or (signal) peptides that are inhibitory to protein translocation.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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