PMID:2193919
| Citation |
Jackowski, S and Alix, JH (1990) Cloning, sequence, and expression of the pantothenate permease (panF) gene of Escherichia coli. J. Bacteriol. 172:3842-8 |
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| Abstract |
Pantothenate permease, the product of the panF gene, catalyzes the sodium-dependent uptake of extracellular pantothenate. The panF gene was isolated from an Escherichia coli genomic DNA library and subcloned into multicopy plasmids. Increased copy number of the panF+ allele resulted in increased rates of pantothenate uptake and a significant increase in the steady-state intracellular pantothenate concentration. Despite the higher levels of pantothenate, the utilization of pantothenate for coenzyme A formation was not elevated, indicating that pantothenate kinase activity is the dominant regulator of coenzyme A biosynthesis. DNA sequencing of the panF gene revealed the presence of a single open reading frame that encoded a hydrophobic protein with a molecular weight of 51,992. Sequence analysis predicts that pantothenate permease is an integral membrane protein possessing 12 hydrophobic membrane-spanning domains connected by short hydrophilic sequences. The predicted topological profile of pantothenate permease is similar to that of other membrane carriers that catalyze cation-dependent symport. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular/methods; DNA, Bacterial/genetics; DNA, Bacterial/isolation & purification; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Gene Expression; Genes, Bacterial; Genotype; Kinetics; Membrane Transport Proteins/genetics; Membrane Transport Proteins/metabolism; Molecular Sequence Data; Organic Anion Transporters; Plasmids; Protein Conformation; Recombinant Proteins/metabolism; Restriction Mapping |
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