SGD Paper 
Anderson DM, et al. (2011) Ubiquitin and ubiquitin-modified proteins activate the Pseudomonas aeruginosa T3SS cytotoxin, ExoU. Mol Microbiol 82(6):1454-67
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.
| Status: Published | Type: Journal Article | PubMed ID: 22040088 |
Topics addressed in this paper
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| Topics | Genes linked to topics |
|---|---|
| SOD1 | |
| Non-Fungal Related Genes/Proteins |  |
| Primary Literature | |
| Protein Processing/Modification/Regulation | |
| Strains/Constructs | |
| Techniques and Reagents | |
