PMID:7783647
| Citation |
Gunn, FJ, Tate, CG, Sansom, CE and Henderson, PJ (1995) Topological analyses of the L-fucose-H+ symport protein, FucP, from Escherichia coli. Mol. Microbiol. 15:771-83 |
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| Abstract |
The transport of L-fucose into Escherichia coli is mediated by the L-fucose-H+ symport protein (FucP). The fucP gene has been sequenced and encodes a hydrophobic protein that contains 438 amino acid residues, with a predicted M(r) of 47,773. The hydropathic profile of FucP indicates 10 to 12 hydrophobic regions that could span the membrane as alpha-helices. A 12-helix model with the N- and C-termini located in the cytoplasm was derived from the hydropathic profile and from application of the 'positive inside' rule. This model was tested using beta-lactamase fusion technology. Analyses of 62 different FucP-beta-lactamase fusions suggested that the FucP protein crosses the cytoplasmic membrane of E. coli 12 times, with the N- and C-termini in the cytoplasm. From measurements of [14C]-L-fucose uptake, it was deduced that the last putative transmembrane region must be complete for transport activity to be retained and that the four C-terminal residues were unnecessary for transport activity. Fourier transform analyses show that all the predicted helices contain a periodicity that enables hydrophobic/hydrophilic faces to be identified; these were particularly evident in putative helices 1, 3, 4, 5, 6, 10 and 11. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Blotting, Western; Carrier Proteins/genetics; Carrier Proteins/physiology; Carrier Proteins/secretion; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Fucose/metabolism; Models, Biological; Molecular Sequence Data; Penicillinase/genetics; Penicillinase/physiology; Protein Structure, Secondary; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/physiology; Structure-Activity Relationship; Symporters; Time Factors |
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