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Vol. 180, Issue 13, 3467-3469, July 1, 1998
1 Department of Molecular Cell Biology and
Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, The
Netherlands,1 and
2 Laboratoire
d'Ingéniérie des Systèmes
Macromoléculaires, CNRS/IBSM, 13402 Marseille Cedex 20, France2
Elastase of Pseudomonas aeruginosa is synthesized as a
preproenzyme. The signal sequence is cleaved off during transport
across the inner membrane and, in the periplasm, proelastase is further processed. We demonstrate that the propeptide and the mature elastase are both secreted but that the propeptide is degraded extracellularly. In addition, reduction of the extracellular proteolytic activity led to
the accumulation of unprocessed forms of LasA and LasD in the
extracellular medium, which shows that these enzymes are secreted in
association with their propeptides. Furthermore, a hitherto undefined
protein with homology to a Streptomyces griseus aminopeptidase accumulated under these conditions.
NOTE
Secretion of Elastinolytic Enzymes and Their
Propeptides by Pseudomonas aeruginosa
Copyright © 1998 by American Society for Microbiology
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