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J Biol Chem, Vol. 273, Issue 46, 30225-30231, November 13, 1998
From the Pseudomonas aeruginosa elastase and
the LasA protease are synthesized as preproenzymes with long
amino-terminal propeptides. The elastase propeptide is cleaved
autocatalytically in the periplasm to form a transient, inactive
elastase-propeptide complex. In contrast, the processing of proLasA
does not involve autoproteolysis. In this study, we analyzed short-term
P. aeruginosa cultures under conditions that minimize
proteolysis and found that an elastase-propeptide complex is secreted,
and then the propeptide is degraded extracellularly, apparently by
elastase itself. LasA protease, on the other hand, was found to be
secreted in its unprocessed 42-kDa proenzyme form. The processing of
proLasA occurred extracellularly, and it involved the transient
appearance of a 28-kDa intermediate and the respective 14-kDa LasA
propeptide fragment. The processing of proLasA in P. aeruginosa strain FRD740, which does not express elastase, also
proceeded via the 28-kDa intermediate, but the rate of processing was
greatly reduced. This low rate of proLasA processing was further reduced when the activity of a secreted lysine-specific protease was
blocked. Purified secreted proteases of P. aeruginosa
(i.e. elastase, the lysine-specific protease, and alkaline
proteinase) converted proLasA to the active enzyme. Processing by
elastase and the lysine-specific enzyme, but not by alkaline
proteinase, proceeded via the 28-kDa intermediate, and both were far
more effective than alkaline proteinase in converting proLasA to the mature enzyme. We conclude that LasA protease and elastase are secreted
with their propeptides, which are then degraded by secreted proteases
of P. aeruginosa. In addition to their other functions, the
propeptides may play a role in targeting their respective enzymes
across the outer membrane.
Elastase and the LasA Protease of Pseudomonas
aeruginosa Are Secreted with Their Propeptides
,,
Maurice and Gabriela Goldschleger Eye
Research Institute, Tel-Aviv University Sackler Faculty of Medicine,
Sheba Medical Center, Tel-Hashomer 52621, Israel and the
¶ Department of Microbiology and Immunology, University of
Tennessee and Veterans Administration Medical Center, Memphis,
Tennessee 38163
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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