PheP, a putative amino acid permease in Staphylococcus aureus, contributes to starvation survival under glucose-limiting conditions and virulence. A pheP mutation led to poor growth after microaerobic or anaerobic incubation on pig serum agar, which was recovered by phenylalanine addition. Genetic complementation of pheP restored growth and starvation survival.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC387907 | PMC |
| http://dx.doi.org/10.1128/IAI.72.5.3073-3076.2004 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
PheP, a putative amino acid permease of Staphylococcus aureus, contributes to survival in vivo and during starvation.
Infect Immun
May 2004
Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield, S10 2TN, United Kingdom.
PheP, a putative amino acid permease in Staphylococcus aureus, contributes to starvation survival under glucose-limiting conditions and virulence. A pheP mutation led to poor growth after microaerobic or anaerobic incubation on pig serum agar, which was recovered by phenylalanine addition. Genetic complementation of pheP restored growth and starvation survival.
View Article and Find Full Text PDFPutative interhelical interactions within the PheP protein revealed by second-site suppressor analysis.
J Bacteriol
November 2003
Department of Microbiology and Immunology, The University of Melbourne, Victoria 3010, Australia.
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.
View Article and Find Full Text PDFTopology of the phenylalanine-specific permease of Escherichia coli.
J Bacteriol
May 1996
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.
View Article and Find Full Text PDFCloning and sequencing of the pheP gene, which encodes the phenylalanine-specific transport system of Escherichia coli.
J Bacteriol
June 1991
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
The phenylalanine-specific permease gene (pheP) of Escherichia coli has been cloned and sequenced. The gene was isolated on a 6-kb Sau3AI fragment from a chromosomal library, and its presence was verified by complementation of a mutant lacking the functional phenylalanine-specific permease. Subcloning from this fragment localized the pheP gene on a 2.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!