This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pi, J. Articles by Pittard, A. J. Search for Related Content PubMed PubMed Citation Articles by Pi, J. Articles by Pittard, A. J.

 Previous Article  |  Next Article 

J. Bacteriol., May 1996, 2650-2655, Vol 178, No. 9
Copyright © 1996, American Society for Microbiology

Topology of the phenylalanine-specific permease of Escherichia coli

J Pi and AJ Pittard
Department of Microbiology, The University of Melbourne, Parkville, Victoria, Australia.

The PheP protein is a high-affinity phenylalanine-specific permease of the bacterium Escherichia coli. A topological model based on sequence analysis of the putative protein in which PheP has 12 transmembrane segments with both N and C termini located in the cytoplasm had been proposed (J. Pi, P. J. Wookey, and A. J. Pittard, J. Bacteriol. 173:3622-3629, 1991). This topological model of PheP has been further examined by generating protein fusions with alkaline phosphatase. Twenty-five sandwich fusion proteins have been constructed by inserting the 'phoA gene at specific sites within the pheP gene. In general, the PhoA activities of the fusions support a PheP topology model consisting of 12 transmembrane segments with the N and C termini in the cytoplasm. However, alterations to the model, affecting spans III and VI, were indicated by this analysis and were supported by additional site- directed mutagenesis of some of the residues involved.

This article has been cited by other articles:

• Zhang, W., Campbell, H. A., King, S. C., Dowhan, W. (2005). 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. 280: 26032-26038 [Abstract] [Full Text]  
• Koyanagi, T., Katayama, T., Suzuki, H., Kumagai, H. (2004). Identification of the LIV-I/LS System as the Third Phenylalanine Transporter in Escherichia coli K-12. J. Bacteriol. 186: 343-350 [Abstract] [Full Text]  
• Zhang, W., Bogdanov, M., Pi, J., Pittard, A. J., Dowhan, W. (2003). Reversible Topological Organization within a Polytopic Membrane Protein Is Governed by a Change in Membrane Phospholipid Composition. J. Biol. Chem. 278: 50128-50135 [Abstract] [Full Text]  
• Dogovski, C., Pi, J., Pittard, A. J. (2003). Putative Interhelical Interactions within the PheP Protein Revealed by Second-Site Suppressor Analysis. J. Bacteriol. 185: 6225-6232 [Abstract] [Full Text]  
• Pi, J., Chow, H., Pittard, A. J. (2002). Study of Second-Site Suppression in the pheP Gene for the Phenylalanine Transporter of Escherichia coli. J. Bacteriol. 184: 5842-5847 [Abstract] [Full Text]  
• Cosgriff, A. J., Brasier, G., Pi, J., Dogovski, C., Sarsero, J. P., Pittard, A. J. (2000). A Study of AroP-PheP Chimeric Proteins and Identification of a Residue Involved in Tryptophan Transport. J. Bacteriol. 182: 2207-2217 [Abstract] [Full Text]  
• van Geest, M., Lolkema, J. S. (2000). Membrane Topology and Insertion of Membrane Proteins: Search for Topogenic Signals. Microbiol. Mol. Biol. Rev. 64: 13-33 [Abstract] [Full Text]  
• Pi, J., Dogovski, C., Pittard, A. J. (1998). Functional Consequences of Changing Proline Residues in the Phenylalanine-Specific Permease of Escherichia coli. J. Bacteriol. 180: 5515-5519 [Abstract] [Full Text]  
• Gilstring, C. F., Ljungdahl, P. O. (2000). A Method for Determining the in Vivo Topology of Yeast Polytopic Membrane Proteins Demonstrates That Gap1p Fully Integrates into the Membrane Independently of Shr3p. J. Biol. Chem. 275: 31488-31495 [Abstract] [Full Text]