Identification of residues in the Pseudomonas aeruginosa elastase propeptide required for chaperone and secretion activities.

@article{McIver2004IdentificationOR,
  title={Identification of residues in the Pseudomonas aeruginosa elastase propeptide required for chaperone and secretion activities.},
  author={Kevin S McIver and Efrat Kessler and Dennis E. Ohman},
  journal={Microbiology},
  year={2004},
  volume={150 Pt 12},
  pages={3969-77}
}
An important virulence factor of the opportunistic human pathogen Pseudomonas aeruginosa is elastase, a secreted thermolysin-like neutral zinc-metalloprotease (TNP). Elastase is synthesized as a larger precursor with an amino-terminal 18 kDa propeptide, and was the first TNP shown to require its propeptide as an intramolecular chaperone (IMC) for activity and secretion. This paper reports the analysis of the elastase propeptide to identify residues conserved among other TNP precursors that may… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 36 references

The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus

R. D. Wetmore, Wong, S.-L, R. S. Roche
Mol Microbiol • 1992
View 4 Excerpts
Highly Influenced

Intramolecular chaperones and protein folding.

Trends in biochemical sciences • 1993
View 4 Excerpts
Highly Influenced

Intramolecular processing of prothermolysin.

The Journal of biological chemistry • 1998
View 2 Excerpts

Pseudolysin (Pseudomonas aeruginosa elastase)

E. Kessler, D. E. Ohman
In Handbook of Proteolytic Enzymes, • 1998
View 2 Excerpts

Propeptide-mediated folding in subtilisin: the intramolecular chaperone concept.

Advances in experimental medicine and biology • 1996
View 1 Excerpt

Similar Papers

Loading similar papers…