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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

C. Dogovski, J. Pi, and A. J. Pittard*

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.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, The University of Melbourne, Victoria 3010, Australia. Phone: 61 3 8344 5696. Fax: 61 3 9347 1540. E-mail: aj.pittard{at}microbiology.unimelb.edu.au.

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.



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