rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1991-7-19
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pubmed:databankReference |
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pubmed:abstractText |
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 2.7-kb HindIII-HindII fragment. The nucleotide sequence of this 2.7-kb region was determined. An open reading frame was identified which extends from a putative start point of translation (GTG at position 636) to a termination signal (TAA at position 2010). The assignment of the GTG as the initiation codon was verified by site-directed mutagenesis of the initiation codon and by introducing a chain termination mutation into the pheP-lacZ fusion construct. A single initiation site of transcription 30 bp upstream of the start point of translation was identified by the primer extension analysis. The pheP structural gene consists of 1,374 nucleotides specifying a protein of 458 amino acid residues. The PheP protein is very hydrophobic (71% nonpolar residues). A topological model predicted from the sequence analysis defines 12 transmembrane segments. This protein is highly homologous with the AroP (general aromatic transport) system of E. coli (59.6% identity) and to a lesser extent with the yeast permeases CAN1 (arginine), PUT4 (proline), and HIP1 (histidine) of Saccharomyces cerevisiae.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1711024-14904456,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1711024-15966102,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1711024-16453726,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1711024-7063399
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems...,
http://linkedlifedata.com/resource/pubmed/chemical/AroP protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Bacterial
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
173
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3622-9
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pubmed:dateRevised |
2010-9-9
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pubmed:meshHeading |
pubmed-meshheading:1711024-Phenylalanine,
pubmed-meshheading:1711024-Escherichia coli,
pubmed-meshheading:1711024-Protein Conformation,
pubmed-meshheading:1711024-Base Sequence,
pubmed-meshheading:1711024-Genes, Bacterial,
pubmed-meshheading:1711024-Protein Biosynthesis,
pubmed-meshheading:1711024-RNA, Bacterial,
pubmed-meshheading:1711024-Bacterial Proteins,
pubmed-meshheading:1711024-Amino Acid Sequence,
pubmed-meshheading:1711024-Biological Transport,
pubmed-meshheading:1711024-Membrane Transport Proteins,
pubmed-meshheading:1711024-Chromosomes, Bacterial,
pubmed-meshheading:1711024-Molecular Sequence Data,
pubmed-meshheading:1711024-Transcription, Genetic,
pubmed-meshheading:1711024-Nucleic Acid Hybridization,
pubmed-meshheading:1711024-Carrier Proteins,
pubmed-meshheading:1711024-Escherichia coli Proteins
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