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ClpXP Protease Regulates the Signal Peptide Cleavage of Secretory Preproteins in Bacillus subtilis with a Mechanism Distinct from That of the Ecs ABC Transporter

Tiina Pummi,¹ Soile Leskelä,¹ Eva Wahlström,^1, Ulf Gerth,² Harold Tjalsma,³ Michael Hecker,² Matti Sarvas,¹ and Vesa P. Kontinen^1*

Vaccine Development Laboratory, National Public Health Institute, FIN-00300 Helsinki, Finland,¹ Institut für Mikrobiologie und Molecularbiologie, Ernst-Moritz-Arndt-Universität, D-17487 Greifswald, Germany,² Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, 9751 NN Haren, The Netherlands³

Received 19 July 2001/ Accepted 19 November 2001

Identification and characterization of a suppressor mutation, sup-15, which partially restored secretion in the protein secretion-deficient Bacillus subtilis ecsA26 mutant, led us to discover a novel function of Clp protease. Inactivation of ClpP improved the processing of the precursor of AmyQ -amylase exposed on the outer surface of the cytoplasmic membrane. A similar improvement of AmyQ secretion was conferred by inactivation of the ClpX substrate-binding component of the ClpXP complex. In the absence of ClpXP, the transcription of the sipS, sipT, sipV, and lsp signal peptidase genes was elevated two- to fivefold, a likely cause of the improvement of the processing and secretion of AmyQ and complementation of ecs mutations. Specific overproduction of SipT enhanced the secretion. These findings extend the regulatory roles of ClpXP to protein secretion. ClpXP also influenced the processing of the lipoprotein PrsA. A concerted regulation of signal peptidase genes by a ClpXP-dependent activator is suggested. In contrast, Ecs did not affect transcription of the sip genes, pointing to a different mechanism of secretion regulation.

Present address: Spectrum Medical Sciences Ltd., FIN-00710 Helsinki, Finland.

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