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J. Biol. Chem., Vol. 276, Issue 28, 26030-26035, July 13, 2001
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From the Department of Molecular Cell Biology and Institute of
Biomembranes, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The
Netherlands
Elastase of Pseudomonas
aeruginosa is synthesized as a preproenzyme. After
propeptide-mediated folding in the periplasm, the proenzyme is
autoproteolytically processed, prior to translocation of both the
mature enzyme and the propeptide across the outer membrane. The
formation of the two disulfide bonds present in the mature enzyme was
examined by studying the expression of the wild-type enzyme and of
alanine for cysteine mutant derivatives in the authentic host and in
dsb mutants of Escherichia coli. It appeared
that the two disulfide bonds are formed successively. First, DsbA
catalyzes the formation of the disulfide bond between Cys-270 and
Cys-297 within the proenzyme. This step is essential for the subsequent
autoproteolytic processing to occur. The second disulfide bond between
Cys-30 and Cys-57 is formed more slowly and appears to be formed after
processing of the proenzyme, and its formation is catalyzed by DsbA as
well. This second disulfide bond appeared to be required for the full
proteolytic activity of the enzyme and contributes to its stability.
Maturation of Pseudomonas aeruginosa Elastase
FORMATION OF THE DISULFIDE BONDS*
,
*
This research was supported by the Netherlands Foundation
for Chemical Research (SON) and by the Life Sciences Foundation (SLW),
which are subsidized by the Netherlands Organization for Scientific
Research (NWO) and by European Community E.U. Grant bio4-CT960119.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.
Present address: Dept. of Pharmaceutical Biology, University of
Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.
§
Present address: Dept. of Gastroenterology and Hepatology, Academic
Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands.
¶
Present address: Dept. of Medical Microbiology, Vrije
Universiteit, Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands.
To whom correspondence should be addressed: Dept. of Molecular
Cell Biology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The
Netherlands. Tel.: 31-30-2532999; Fax: 31-30-2513655; E-mail: j.p.m. tommassen@bio.uu.nl.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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