JBC PeproTech; Our Business is Cytokines!

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on January 23, 2004
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
279/4/2747    most recent
M301963200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Krall, R.
Right arrow Articles by Barbieri, J. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Krall, R.
Right arrow Articles by Barbieri, J. T.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print November 3, 2003
J. Biol. Chem, 10.1074/jbc.M301963200
Submitted on February 25, 2003
Revised on November 3, 2003
Accepted on November 3, 2003

Intracellular membrane localization of Pseudomonas ExoS and Yersinia YopE in mammalian cells

Rebecca Krall, Yue Zhang, and Joseph T. Barbieri

Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226

Corresponding Author: jtb01{at}mcw.edu

ExoS (453 amino acids) is a bi-functional type-III cytotoxin of Pseudomonas aeruginosa. Residues 96-233 comprise the Rho GTPase Activating Protein (Rho GAP) domain, while residues 234-453 comprise the 14-3-3 dependent ADP-ribosyltransferase domain. Residues 51-72 represent a membrane localization domain (MLD), which targets ExoS to peri-nuclear vesicles within mammalian cells. YopE (219 amino acids) is a type-III cytotoxin of Yersinia that is also a Rho GAP. Residues 96 to 219 comprise the YopE Rho GAP domain. While the Rho GAP domains of ExoS and YopE share structural homology, unlike ExoS, the intracellular localization of YopE within mammalian cells has not been resolved and is the subject of this nvestigation. Deletion mapping showed that the N terminus of YopE was required for intracellular membrane localization of YopE in CHO cells. A fusion protein containing the N-terminal 84 amino acids of YopE localized to a punctuate-perinuclear region in mammalian cells and co-localized with a fusion protein containing the MLD of ExoS. Residues 54-75 of YopE (termed YopE-MLD) were necessary and sufficient for intracellular localization in mammalian cells. The YopE-MLD localized ExoS to intracellular membranes and targeted ExoS to ADP-ribosylate small molecular weight membrane proteins as observed for native type-III delivered ExoS. These data indicate that the YopE MLD functionally complements the ExoS MLD for intracellular targeting in mammalian cells.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
L. Rodgers, A. Gamez, R. Riek, and P. Ghosh
The Type III Secretion Chaperone SycE Promotes a Localized Disorder-to-Order Transition in the Natively Unfolded Effector YopE
J. Biol. Chem., July 25, 2008; 283(30): 20857 - 20863.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Zhang, Q. Deng, and J. T. Barbieri
Intracellular Localization of Type III-delivered Pseudomonas ExoS with Endosome Vesicles
J. Biol. Chem., April 27, 2007; 282(17): 13022 - 13032.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
J. Jia, Y. Wang, L. Zhou, and S. Jin
Expression of Pseudomonas aeruginosa Toxin ExoS Effectively Induces Apoptosis in Host Cells
Infect. Immun., December 1, 2006; 74(12): 6557 - 6570.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
K. Ruckdeschel, G. Pfaffinger, K. Trulzsch, G. Zenner, K. Richter, J. Heesemann, and M. Aepfelbacher
The Proteasome Pathway Destabilizes Yersinia Outer Protein E and Represses Its Antihost Cell Activities
J. Immunol., May 15, 2006; 176(10): 6093 - 6102.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
S. D. P. Rabin, J. L. Veesenmeyer, K. T. Bieging, and A. R. Hauser
A C-Terminal Domain Targets the Pseudomonas aeruginosa Cytotoxin ExoU to the Plasma Membrane of Host Cells.
Infect. Immun., May 1, 2006; 74(5): 2552 - 2561.
[Abstract] [Full Text] [PDF]

Home page
 Infect. Immun.Home page
Y. Zhang and J. T. Barbieri
A Leucine-Rich Motif Targets Pseudomonas aeruginosa ExoS within Mammalian Cells
Infect. Immun., December 1, 2005; 73(12): 7938 - 7945.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Q. Deng, J. Sun, and J. T. Barbieri
Uncoupling Crk Signal Transduction by Pseudomonas Exoenzyme T
J. Biol. Chem., October 28, 2005; 280(43): 35953 - 35960.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
P. Ghosh
Process of Protein Transport by the Type III Secretion System
Microbiol. Mol. Biol. Rev., December 1, 2004; 68(4): 771 - 795.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. W. Maresso, M. R. Baldwin, and J. T. Barbieri
Ezrin/Radixin/Moesin Proteins Are High Affinity Targets for ADP-ribosylation by Pseudomonas aeruginosa ExoS
J. Biol. Chem., September 10, 2004; 279(37): 38402 - 38408.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.