We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU.
- Authors
Anderson, David M; Schmalzer, Katherine M; Sato, Hiromi; Casey, Monika; Terhune, Scott S; Haas, Arthur L; Feix, Jimmy B; Frank, Dara W
- Abstract
Pseudomonas aeruginosa is an opportunistic Gram-negative pathogen that possesses a type III secretion system (T3SS) critical for evading innate immunity and establishing acute infections in compromised patients. Our research has focused on the structure-activity relationships of ExoU, the most toxic and destructive type III effector produced by P. aeruginosa. ExoU possesses phospholipase activity, which is detectable in vitro only when a eukaryotic cofactor is provided with membrane substrates. We report here that a subpopulation of ubiquitylated yeast SOD1 and other ubiquitylated mammalian proteins activate ExoU. Phospholipase activity was detected using purified ubiquitin of various chain lengths and linkage types; however, free monoubiquitin is sufficient in a genetically engineered dual expression system. The use of ubiquitin by a bacterial enzyme as an activator is unprecedented and represents a new aspect in the manipulation of the eukaryotic ubiquitin system to facilitate bacterial replication and dissemination.
- Publication
Molecular microbiology, 2011, Vol 82, Issue 6, p1454
- ISSN
1365-2958
- Publication type
Journal Article
- DOI
10.1111/j.1365-2958.2011.07904.x