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Vol. 12, No. 15, pp. 2318-2331, August 1, 1998
1 Department of Genetics, Groningen Biomolecular Sciences
and Biotechnology Institute, University of Groningen, 9751 NN Haren,
The Netherlands;
2 Institute of Genetics, University of
Bayreuth, D-95440 Bayreuth, Germany;
3 Genencor International,
2288 GJ Rijswijk, The Netherlands;
4 Department of
Pharmaceutical Biology, University of Groningen, 9713 AV Groningen,
The Netherlands
Approximately 47% of the genes of the Gram-positive bacterium
Bacillus subtilis belong to paralogous gene families. The
present studies were aimed at the functional analysis of the
sip gene family of B. subtilis, consisting of five
chromosomal genes, denoted sipS, sipT, sipU, sipV, and
sipW. All five sip genes specify type I signal
peptidases (SPases), which are actively involved in the processing of
secretory preproteins. Interestingly, strains lacking as many as four
of these SPases could be obtained. As shown with a
temperature-sensitive SipS variant, only cells lacking both SipS and
SipT were not viable, which may be caused by jamming of the secretion
machinery with secretory preproteins. Thus, SipS and SipT are of major
importance for protein secretion. This conclusion is underscored by the
observation that only the transcription of the sipS and
sipT genes is temporally controlled via the DegS-DegU regulatory system, in concert with the transcription of most genes for
secretory preproteins. Notably, the newly identified SPase SipW is
highly similar to SPases from archaea and the ER membrane of
eukaryotes, suggesting that these enzymes form a subfamily of the type
I SPases, which is conserved in the three domains of life.
[Key Words: Bacillus subtilis; paralogous gene family; protein secretion; signal peptidase; leader peptidase]
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