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J. Biol. Chem., Vol. 275, Issue 33, 25102-25108, August 18, 2000
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From the Type I signal peptidases (SPases) are required
for the removal of signal peptides from translocated proteins and,
subsequently, release of the mature protein from the trans
side of the membrane. Interestingly, prokaryotic (P-type) and
endoplasmic reticular (ER-type) SPases are functionally equivalent, but
structurally quite different, forming two distinct SPase families that
share only few conserved residues. P-type SPases were, so far,
exclusively identified in eubacteria and organelles, whereas ER-type
SPases were found in the three kingdoms of life. Strikingly, the
presence of ER-type SPases appears to be limited to sporulating
Gram-positive eubacteria. The present studies were aimed at the
identification of potential active site residues of the ER-type SPase
SipW of Bacillus subtilis, which is required for processing
of the spore-associated protein TasA. Conserved serine, histidine, and
aspartic acid residues are critical for SipW activity, suggesting that
the ER-type SPases employ a Ser-His-Asp catalytic triad or,
alternatively, a Ser-His catalytic dyad. In contrast, the P-type SPases
employ a Ser-Lys catalytic dyad (Paetzel, M., Dalbey, R. E., and
Strynadka, N. C. J. (1998) Nature 396, 186-190).
Notably, catalytic activity of SipW was not only essential for pre-TasA
processing, but also for the incorporation of mature TasA into spores.
Conserved Serine and Histidine Residues Are Critical for
Activity of the ER-type Signal Peptidase SipW of Bacillus
subtilis*
§,
**,
,
,

, and

§§
Department of Genetics, Groningen
Biomolecular Sciences and Biotechnology Institute, Kerklaan 30, 9751 NN Haren, The Netherlands and the ¶ Department of
Microbiology and Immunology, Loyola University Medical Center,
Maywood, Illinois 60153
*
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.
Supported by Public Health Service Grant GM539898 from the
National Institutes of Health and a grant from the Schweppe Foundation.
**
Supported in part by a Schmitt fellowship.

Supported by Biotechnology Grants Bio4-CT95-0278 and
Bio4-CT96-0097 and "Quality of Life and Management of Living
Resources" Grants QLK3-CT-1999-00415 and QLK3-CT-1999-00917 from the
European Union.
§§
To whom correspondence should be addressed. Present address:
Dept. of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands. Tel.:
31-503633079; Fax: 31-503632348; E-mail:
j.m.van.dijl@farm.rug.nl.
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