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Vol. 180, Issue 13, 3467-3469, July 1, 1998

NOTE
Secretion of Elastinolytic Enzymes and Their Propeptides by Pseudomonas aeruginosa

Peter Braun1, Arjan de Groot2, Wilbert Bitter1, and Jan Tommassen1

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.

Copyright © 1998 by American Society for Microbiology


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