Intracellular Membrane Localization of Pseudomonas ExoS and Yersinia YopE in Mammalian Cells
نویسندگان
چکیده
منابع مشابه
The membrane localization domain is required for intracellular localization and autoregulation of YopE in Yersinia pseudotuberculosis.
Recent work has shown that a domain of YopE of Yersinia pseudotuberculosis ranging from amino acids 54 to 75 (R. Krall, Y. Zhang, and J. T. Barbieri, J. Biol. Chem. 279:2747-2753, 2004) is required for proper localization of YopE after ectopic expression in eukaryotic cells. This domain, called the membrane localization domain (MLD), has not been extensively studied in Yersinia. Therefore, an i...
متن کاملMicroinjection of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption.
Introduction Three species of the genus Yersinia may produce disease in humans: they are Y. pestis, Y. pseudotuberculosis and Y. enterocolitica. Y pseudotuberculosis may cause fatal infection in rodents but produces only mild gastrointestinal disease in humans. Pathogenic Yersinia possess a common virulence plasmid of about 70 kb in size. Upon incubation at 37°C in the absence of CaZ+ ions, str...
متن کاملMembrane localization contributes to the in vivo ADP-ribosylation of Ras by Pseudomonas aeruginosa ExoS.
Type III-delivered exoenzyme S (ExoS) preferentially ADP-ribosylated membrane-associated His(6)HRas, relative to its cytosolic derivative His(6)HRas Delta CAAX. This indicates that the subcellular protein distribution contributes to in vivo ADP-ribosylation by ExoS.
متن کاملA leucine-rich motif targets Pseudomonas aeruginosa ExoS within mammalian cells.
Type III cytotoxins contribute to the ability of bacterial pathogens to subvert the host innate immune system. ExoS (453 amino acids) is a bifunctional type III cytotoxin produced by Pseudomonas aeruginosa. Residues 96 to 232 comprise a Rho GTPase activating protein domain, while residues 233 to 453 comprise a 14-3-3-dependent ADP-ribosyltransferase domain. An N-terminal domain (termed the memb...
متن کاملIntracellular localization of phospholipase D1 in mammalian cells.
Phospholipase D (PLD) hydrolyzes phosphatidylcholine to generate phosphatidic acid. In mammalian cells this reaction has been implicated in the recruitment of coatomer to Golgi membranes and release of nascent secretory vesicles from the trans-Golgi network. These observations suggest that PLD is associated with the Golgi complex; however, to date, because of its low abundance, the intracellula...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m301963200