This Article Full Text 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 Dogovski, C. Articles by Pittard, A. J. Search for Related Content PubMed PubMed Citation Articles by Dogovski, C. Articles by Pittard, A. J.

Next Article 

Journal of Bacteriology, November 2003, p. 6225-6232, Vol. 185, No. 21
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.21.6225-6232.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Putative Interhelical Interactions within the PheP Protein Revealed by Second-Site Suppressor Analysis

Department of Microbiology and Immunology, The University of Melbourne, Victoria 3010, Australia

Received 17 March 2003/ Accepted 30 July 2003

Highly conserved glycine residues within span I and span II of the phenylalanine and tyrosine transporter PheP were shown to be important for the function of the wild-type protein. Replacement by amino acids with increasing side chain volume led to progressive loss of transport activity. Second-site suppression studies performed with a number of the primary mutants revealed a tight packing arrangement between spans I and II that is important for function and an additional interaction between spans I and III. We also postulate that a third motif, GXXIG, present in span I and highly conserved within different members of the amino acid-polyamine-organocation family, may function as a dimerization motif. Surprisingly, other highly conserved residues, such as Y60 and L41, could be replaced by various residues with no apparent loss of activity.

This article has been cited by other articles:

• Xie, J., Bogdanov, M., Heacock, P., Dowhan, W. (2006). Phosphatidylethanolamine and Monoglucosyldiacylglycerol Are Interchangeable in Supporting Topogenesis and Function of the Polytopic Membrane Protein Lactose Permease. J. Biol. Chem. 281: 19172-19178 [Abstract] [Full Text]  
• Ramirez-Arcos, S., Greco, V., Douglas, H., Tessier, D., Fan, D., Szeto, J., Wang, J., Dillon, J. R. (2004). Conserved Glycines in the C Terminus of MinC Proteins Are Implicated in Their Functionality as Cell Division Inhibitors. J. Bacteriol. 186: 2841-2855 [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]