Advertisement
JBC

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


     


Originally published In Press as doi:10.1074/jbc.M309840200 on October 1, 2003

J. Biol. Chem., Vol. 278, Issue 50, 50128-50135, December 12, 2003
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
278/50/50128    most recent
M309840200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhang, W.
Right arrow Articles by Dowhan, W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhang, W.
Right arrow Articles by Dowhan, W.
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?

Reversible Topological Organization within a Polytopic Membrane Protein Is Governed by a Change in Membrane Phospholipid Composition*

Wei Zhang{ddagger}, Mikhail Bogdanov{ddagger}, Jing Pi§, A. James Pittard§, and William Dowhan{ddagger}

From the {ddagger}Department of Biochemistry and Molecular Biology, University of Texas, Medical School and Graduate School of Biomedical Sciences, Houston, Texas 77030 and the §Department of Microbiology and Immunology, University of Melbourne, Victoria 3010, Australia

Once inserted, transmembrane segments of polytopic membrane proteins are generally considered stably oriented due to the large free energy barrier to topological reorientation of adjacent extramembrane domains. However, the topology and function of the polytopic membrane protein lactose permease of Escherichia coli are dependent on the membrane phospholipid composition, revealing topological dynamics of transmembrane domains after stable membrane insertion (Bogdanov, M., Heacock, P. N., and Dowhan, W. (2002) EMBO J. 21, 2107–2116). In this study, we show that the high affinity phenylalanine permease PheP shares many similarities with lactose permease. PheP assembled in a mutant of E. coli lacking phosphatidylethanolamine (PE) exhibited significantly reduced active transport function and a complete inversion in topological orientation of the N terminus and adjoining transmembrane hairpin loop compared with PheP in a PE-containing strain. Introduction of PE following the assembly of PheP triggered a reorientation of the N terminus and adjacent hairpin to their native orientation associated with regain of wild-type transport function. The reversible orientation of these secondary transport proteins in response to a change in phospholipid composition might be a result of inherent conformational flexibility necessary for transport function or during protein assembly.


Received for publication, September 4, 2003 , and in revised form, October 1, 2003.

* This work was supported in part by National Institutes of Health Grant GM20487 (to W. D.) and the Australian Research Council Large Grants Scheme (to A. J. P.). 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.

To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, University of Texas Medical School, 6431 Fannin St., Suite 6.200, P. O. Box 20708, Houston, TX 77030. Tel.: 713-500-6051; Fax: 713-500-0652; E-mail: William.Dowhan{at}uth.tmc.edu.


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
M. Bogdanov, J. Xie, and W. Dowhan
Lipid-Protein Interactions Drive Membrane Protein Topogenesis in Accordance with the Positive Inside Rule
J. Biol. Chem., April 10, 2009; 284(15): 9637 - 9641.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
W. Dowhan
Molecular genetic approaches to defining lipid function
J. Lipid Res., April 1, 2009; 50(Supplement): S305 - S310.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Wikstrom, A. A. Kelly, A. Georgiev, H. M. Eriksson, M. R. Klement, M. Bogdanov, W. Dowhan, and A. Wieslander
Lipid-engineered Escherichia coli Membranes Reveal Critical Lipid Headgroup Size for Protein Function
J. Biol. Chem., January 9, 2009; 284(2): 954 - 965.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
M. Bogdanov, J. Xie, P. Heacock, and W. Dowhan
To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane protein topology
J. Cell Biol., September 9, 2008; 182(5): 925 - 935.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Soto and G. M. Carman
Regulation of the Saccharomyces cerevisiae CKI1-encoded Choline Kinase by Zinc Depletion
J. Biol. Chem., April 11, 2008; 283(15): 10079 - 10088.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. Hakizimana, M. Masureel, B. Gbaguidi, J.-M. Ruysschaert, and C. Govaerts
Interactions between Phosphatidylethanolamine Headgroup and LmrP, a Multidrug Transporter: A CONSERVED MECHANISM FOR PROTON GRADIENT SENSING?
J. Biol. Chem., April 4, 2008; 283(14): 9369 - 9376.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Xie, M. Bogdanov, P. Heacock, and W. Dowhan
Phosphatidylethanolamine and Monoglucosyldiacylglycerol Are Interchangeable in Supporting Topogenesis and Function of the Polytopic Membrane Protein Lactose Permease
J. Biol. Chem., July 14, 2006; 281(28): 19172 - 19178.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. Zhang, H. A. Campbell, S. C. King, and W. Dowhan
Phospholipids as Determinants of Membrane Protein Topology: PHOSPHATIDYLETHANOLAMINE IS REQUIRED FOR THE PROPER TOPOLOGICAL ORGANIZATION OF THE {gamma}-AMINOBUTYRIC ACID PERMEASE (GabP) OF ESCHERICHIA COLI
J. Biol. Chem., July 15, 2005; 280(28): 26032 - 26038.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. A. Dodd, B. Niederoest, S. Bloechlinger, L. Dupuis, J.-P. Loeffler, and M. E. Schwab
Nogo-A, -B, and -C Are Found on the Cell Surface and Interact Together in Many Different Cell Types
J. Biol. Chem., April 1, 2005; 280(13): 12494 - 12502.
[Abstract] [Full Text] [PDF]


Home page
Arterioscler. Thromb. Vasc. Bio.Home page
V. Llorente-Cortes and L. Badimon
LDL Receptor-Related Protein and the Vascular Wall: Implications for Atherothrombosis
Arterioscler. Thromb. Vasc. Biol., March 1, 2005; 25(3): 497 - 504.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
T. P. Roosild, J. Greenwald, M. Vega, S. Castronovo, R. Riek, and S. Choe
NMR Structure of Mistic, a Membrane-Integrating Protein for Membrane Protein Expression
Science, February 25, 2005; 307(5713): 1317 - 1321.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
S. H. Kim, A. B. Chang, and M. H. Saier Jr
Sequence similarity between multidrug resistance efflux pumps of the ABC and RND superfamilies
Microbiology, August 1, 2004; 150(8): 2493 - 2495.
[Full Text] [PDF]


Home page
CirculationHome page
V. Llorente-Cortes, M. Otero-Vinas, S. Camino-Lopez, O. Llampayas, and L. Badimon
Aggregated Low-Density Lipoprotein Uptake Induces Membrane Tissue Factor Procoagulant Activity and Microparticle Release in Human Vascular Smooth Muscle Cells
Circulation, July 27, 2004; 110(4): 452 - 459.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Wikstrom, J. Xie, M. Bogdanov, E. Mileykovskaya, P. Heacock, A. Wieslander, and W. Dowhan
Monoglucosyldiacylglycerol, a Foreign Lipid, Can Substitute for Phosphatidylethanolamine in Essential Membrane-associated Functions in Escherichia coli
J. Biol. Chem., March 12, 2004; 279(11): 10484 - 10493.
[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 © 2003 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement