ArticleJournal of bacteriology1998
Functional consequences of changing proline residues in the phenylalanine-specific permease of Escherichia coli.
Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- UBCH5 Family Members Differentially Impact Stabilization of Mutant p53 via RNF128 Iso1 During Barrett's Progression to Esophageal Adenocarcinoma.Cellular and molecular gastroenterology and hepatology · 2022Article
- Quaternary structure of the small amino acid transporter OprG fromThe Journal of biological chemistry · 2018Article
- Biochemical and pathological changes result from mutated Caveolin-3 in muscle.Skeletal muscle · 2018Article
- Genetic variation in CYP3A43 is associated with response to antipsychotic medication.Journal of neural transmission (Vienna, Austria : 1996) · 2015Review
- Identification of critical residues of the serotype modifying O-acetyltransferase of Shigella flexneri.BMC biochemistry · 2012Article
- Secondary transport of amino acids in prokaryotes.The Journal of membrane biology · 2006Review
- Putative interhelical interactions within the PheP protein revealed by second-site suppressor analysis.Journal of bacteriology · 2003Article
- Study of second-site suppression in the pheP gene for the phenylalanine transporter of Escherichia coli.Journal of bacteriology · 2002Article
- A study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport.Journal of bacteriology · 2000Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The PheP protein is a high-affinity phenylalanine-specific permease of the bacterium Escherichia coli. A topological model based on genetic analysis involving the construction of protein fusions with alkaline phosphatase has previously been proposed in which PheP has 12 transmembrane segments with both N and C termini located in the cytoplasm (J. Pi and A. J. Pittard, J. Bacteriol. 178:2650-2655, 1996). Site-directed mutagenesis has been used to investigate the functional importance of each of the 16 proline residues of the PheP protein. Replacement of alanine at only three positions, P54, P341, and P442, resulted in the loss of 50% or more activity. Substitutions at P341 had the most dramatic effects. None of these changes in transport activity were, however, associated with any defect of the mutant protein in inserting into the membrane, as indicated by [35S]methionine labelling and immunoprecipitation using anti-PheP serum. A possible role for each of these three prolines is discussed. Inserting a single alanine residue at different sites within span IX and the loop immediately preceding it also had major effects on transport activity, suggesting an important role for a highly organized structure in this region of the protein.
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