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Journal of Bacteriology, April 1999, p. 2448-2454, Vol. 181, No. 8
Department of Genetics, Groningen
Biomolecular Sciences and Biotechnology Institute, University of
Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
Received 5 November 1998/Accepted 1 February 1999
The gram-positive eubacterium Bacillus subtilis is the
organism with the largest number of paralogous type I signal peptidases (SPases) known. These are specified both by chromosomal and
plasmid-borne genes. The chromosomally encoded SPases SipS and SipT
have a major function in precursor processing, and cells depleted of
SipS and SipT stop growing and die. In this study, we show that the
SPase SipP, specified by the B. subtilis plasmid pTA1015,
can functionally replace SipS and SipT, unlike the three chromosomally
encoded SPases with a minor function in protein secretion (i.e., SipU, SipV, and SipW). Unexpectedly, SipP is not specifically required for
the processing and secretion of Orf1p, which is specified by a gene
that is cotranscribed with sipP. These two genes form a
conserved structural module of rolling-circle plasmids from B. subtilis. As previously shown for the chromosomal
sipS and sipT genes, the transcription of
plasmid-borne copies of sipP is temporally controlled,
reaching maximal levels during the post-exponential growth phase when
the cells secrete proteins at high levels. However, increased
transcription of sipP starts at the end of exponential growth, about 2 h earlier than that of sipS and
sipT. These data suggest that SipP fulfills a general role
in the secretory precursor processing of pTA1015-containing cells.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The Plasmid-Encoded Signal Peptidase SipP Can
Functionally Replace the Major Signal Peptidases SipS and SipT of
Bacillus subtilis

*
Corresponding author. Present address: Department of
Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. Phone: 31503633079. Fax: 31503632348. E-mail: J.M.VAN.DIJL{at}FARM.RUG.NL.
Present address: Centro de Biología Molecular "Severo
Ochoa" (CSIC-UAM), Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain.
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