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J. Biol. Chem., Vol. 278, Issue 17, 14739-14746, April 25, 2003
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From the Department of Genetics, University of Groningen, Groningen
Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN Haren, The Netherlands
Lipid-modified proteins play important roles at
the interface between eubacterial cells and their environment. The
importance of lipoprotein processing by signal peptidase II (SPase II)
is underscored by the fact that this enzyme is essential for viability of the Gram-negative eubacterium Escherichia coli. In
contrast, SPase II is not essential for growth and viability of the
Gram-positive eubacterium Bacillus subtilis. This could be
due to alternative amino-terminal lipoprotein processing, which was
shown previously to occur in SPase II mutants of B. subtilis. Alternatively, uncleaved lipoprotein precursors might
be functional. To explore further the importance of lipoprotein
processing in Gram-positive eubacteria, an SPase II mutant strain of
Lactococcus lactis was constructed. Although some of the 39 (predicted) lactococcal lipoproteins, such as PrtM and OppA, are
essential for growth in milk, the growth of SPase II mutant L. lactis cells in this medium was not affected. Furthermore, the
activity of the strictly PrtM-dependent extracellular protease PrtP, which is required for casein degradation, was not impaired in the absence of SPase II. Importantly, no alternative processing of pre-PrtM and pre-OppA was observed in cells lacking SPase
II. Taken together, these findings show for the first time that
authentic lipoprotein precursors retain biological activity.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) U63724.
Active Lipoprotein Precursors in the Gram-positive Eubacterium
Lactococcus lactis*
,
,
, and
*
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.
This paper is dedicated to the memory of Roelke Venema. We
recall sunny and cheerful days with Roelke in our midst.
Supported by Genencor International, Inc. (Leiden, The Netherlands).
§
Supported by Grants Bio2-CT93-0254, QLK3-CT-1999-00413 and
QLK3-CT-1999-00917 from the European Union. Present address: Dept. of
Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.
¶
Present address: BioMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Performed this work as a part of the STARLAB Project (Contract
BIO4-CT96-0016) of the European Union. To whom correspondence should be
addressed. Tel.: 31-50-3632287; Fax: 31-50-3632348; E-mail:
Buistg@biol.rug.nl.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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