JBC Biosymposia, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M504371200 on June 24, 2005

J. Biol. Chem., Vol. 280, Issue 34, 30310-30319, August 26, 2005
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental data
Right arrow All Versions of this Article:
280/34/30310    most recent
M504371200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Cuthbertson, L.
Right arrow Articles by Whitfield, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cuthbertson, L.
Right arrow Articles by Whitfield, C.
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?

The C-terminal Domain of the Nucleotide-binding Domain Protein Wzt Determines Substrate Specificity in the ATP-binding Cassette Transporter for the Lipopolysaccharide O-antigens in Escherichia coli Serotypes O8 and O9a*{boxs}

Leslie Cuthbertson{ddagger}, Jacqueline Powers§, and Chris Whitfield, Recipient of a Tier 1 Canada Research Chair¶

From the Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada

The polymannan O-antigenic polysaccharides (O-PSs) of Escherichia coli O8 and O9a are synthesized via an ATP-binding cassette (ABC) transporter-dependent pathway. The group 2 capsular polysaccharides of E. coli serve as prototypes for polysaccharide synthesis and export via this pathway. Here, we show that there are some fundamental differences between the ABC transporter-dependent pathway for O-PS biosynthesis and the capsular polysaccharide paradigm. In the capsule system, mutants lacking the ABC transporter are viable, and membranes isolated from these strains are no longer able to synthesize polymer using an endogenous acceptor. In contrast, E. coli strains carrying mutations in the membrane component (Wzm) and/or the nucleotide-binding component (Wzt) of the O8 and O9a polymannan transporters are nonviable under conditions permissive to O-PS biosynthesis and take on an aberrant elongated cell morphology. Whereas the ABC transporters for capsular polysaccharides with different structures are functionally interchangeable, the O8 and O9a exporters are specific for their cognate polymannan substrates. The E. coli O8 and O9a Wzt proteins contain a C-terminal domain not present in the corresponding nucleotide-binding protein (KpsT) from the capsule exporter. Whereas the Wzm components are functionally interchangeable, albeit with reduced efficiency, the Wzt components are not, indicating a specific role for Wzt in substrate specificity. Chimeric Wzt proteins were constructed in order to localize the region involved in substrate specificity to the C-terminal domain.


Received for publication, April 21, 2005 , and in revised form, June 2, 2005.

* This work was supported by Canadian Institutes of Health Research Grant MOP-62877 (to C. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{boxs} The on-line version of this article (available at http://www.jbc.org) contains Tables 2 and 3.

{ddagger} Recipient of a Postgraduate Scholarship (PGS-A) from the Natural Sciences and Engineering Research Council.

§ Recipient of a Canadian Institutes for Health Research Postdoctoral Fellowship.

To whom correspondence should be addressed: Dept. of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada. Tel.: 519-824-4120 (ext. 53361); Fax: 519-837-1802; E-mail: cwhitfie{at}uoguelph.ca.


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
K. Steiner, R. Novotny, D. B. Werz, K. Zarschler, P. H. Seeberger, A. Hofinger, P. Kosma, C. Schaffer, and P. Messner
Molecular Basis of S-layer Glycoprotein Glycan Biosynthesis in Geobacillus stearothermophilus
J. Biol. Chem., July 25, 2008; 283(30): 21120 - 21133.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
A. L. Davidson, E. Dassa, C. Orelle, and J. Chen
Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems
Microbiol. Mol. Biol. Rev., June 1, 2008; 72(2): 317 - 364.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
L. Cuthbertson, M. S. Kimber, and C. Whitfield
Substrate binding by a bacterial ABC transporter involved in polysaccharide export
PNAS, December 4, 2007; 104(49): 19529 - 19534.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
S. Berg, D. Kaur, M. Jackson, and P. J Brennan
The glycosyltransferases of Mycobacterium tuberculosis--roles in the synthesis of arabinogalactan, lipoarabinomannan, and other glycoconjugates
Glycobiology, June 1, 2007; 17(6): 35R - 56R.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
M. A. D'Elia, M. P. Pereira, Y. S. Chung, W. Zhao, A. Chau, T. J. Kenney, M. C. Sulavik, T. A. Black, and E. D. Brown
Lesions in Teichoic Acid Biosynthesis in Staphylococcus aureus Lead to a Lethal Gain of Function in the Otherwise Dispensable Pathway.
J. Bacteriol., June 1, 2006; 188(12): 4183 - 4189.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
M. Wacker, M. F. Feldman, N. Callewaert, M. Kowarik, B. R. Clarke, N. L. Pohl, M. Hernandez, E. D. Vines, M. A. Valvano, C. Whitfield, et al.
Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems
PNAS, May 2, 2006; 103(18): 7088 - 7093.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.