Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 6, Pages 4311-4322Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.310300
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Funding
- National Institutes of Health, NIDDK [DK083284, DK072506]
- University of Pittsburgh School of Medicine, Department of Cell Biology and Physiology
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Pseudomonas aeruginosa is an opportunistic pathogen that contributes to the mortality of immunocompromised individuals and patients with cystic fibrosis. Pseudomonas infection presents clinical challenges due to its ability to form biofilms and modulate host-pathogen interactions through the secretion of virulence factors. The calcium-regulated alkaline protease (AP), a member of the repeats in toxin (RTX) family of proteins, is implicated in multiple modes of infection. A series of full-length and truncation mutants were purified for structural and functional studies to evaluate the role of Ca2+ in AP folding and activation. We find that Ca2+ binding induces RTX folding, which serves to chaperone the folding of the protease domain. Subsequent association of the RTX domain with an N-terminal alpha-helix stabilizes AP. These results provide a basis for the Ca2+-mediated regulation of AP and suggest mechanisms by which Ca2+ regulates the RTX family of virulence factors.
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