PMID:1702779: Difference between revisions

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<span style = 'font-size: large'> '''Olson, ER, Dunyak, DS, Jurss, LM and Poorman, RA'''  (1991) Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein.''J. Bacteriol.'' '''173''':234-44</span>
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!align=left  |Citation
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'''Olson, ER, Dunyak, DS, Jurss, LM and Poorman, RA'''  (1991) Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein. ''J. Bacteriol.'' '''173''':234-44
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!align=left  |Abstract
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We describe the isolation and analysis of an Escherichia coli gene, dppA, and its role in dipeptide transport. dppA maps near min 79 and encodes a protein (DppA) that has regions of amino acid similarity with a peptide-binding protein from Salmonella typhimurium (OppA). Like OppA, DppA is found in the periplasmic space and thus is most likely a dipeptide-binding protein. Insertional inactivation of dppA results in the inability of a proline auxotroph to utilize Pro-Gly as a proline source. dppA-dependent Pro-Gly utilization does not require any of the three major proline transport systems, demonstrating that DppA is not simply a dipeptidase. An in vivo competition assay was used to show that DppA is probably involved in the transport of dipeptides other than Pro-Gly. Transcription of dppA is repressed by the presence of casamino acids, suggesting that the cell alters its dipeptide transport capabilities in response to an environmental signal.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1702779 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC207180 PMC207180]


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|{{TableHeadingColor}} |'''Abstract''' || We describe the isolation and analysis of an Escherichia coli gene, dppA, and its role in dipeptide transport. dppA maps near min 79 and encodes a protein (DppA) that has regions of amino acid similarity with a peptide-binding protein from Salmonella typhimurium (OppA). Like OppA, DppA is found in the periplasmic space and thus is most likely a dipeptide-binding protein. Insertional inactivation of dppA results in the inability of a proline auxotroph to utilize Pro-Gly as a proline source. dppA-dependent Pro-Gly utilization does not require any of the three major proline transport systems, demonstrating that DppA is not simply a dipeptidase. An in vivo competition assay was used to show that DppA is probably involved in the transport of dipeptides other than Pro-Gly. Transcription of dppA is repressed by the presence of casamino acids, suggesting that the cell alters its dipeptide transport capabilities in response to an environmental signal.
!align=left  |Keywords
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Amino Acid Sequence; Bacterial Proteins/genetics; Bacteriophage lambda/genetics; Base Sequence; Biological Transport; Blotting, Northern; Carrier Proteins/genetics; DNA, Bacterial/genetics; DNA, Bacterial/isolation & purification; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Genes, Bacterial; Membrane Transport Proteins/genetics; Molecular Sequence Data; Nucleic Acid Hybridization; Oligonucleotide Probes; Periplasmic Binding Proteins; Plasmids; RNA, Bacterial/genetics; RNA, Bacterial/isolation & purification; Restriction Mapping; Sequence Homology, Nucleic Acid
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1702779 PubMed]
 
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Latest revision as of 04:30, 15 September 2013

Citation

Olson, ER, Dunyak, DS, Jurss, LM and Poorman, RA (1991) Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein. J. Bacteriol. 173:234-44

Abstract

We describe the isolation and analysis of an Escherichia coli gene, dppA, and its role in dipeptide transport. dppA maps near min 79 and encodes a protein (DppA) that has regions of amino acid similarity with a peptide-binding protein from Salmonella typhimurium (OppA). Like OppA, DppA is found in the periplasmic space and thus is most likely a dipeptide-binding protein. Insertional inactivation of dppA results in the inability of a proline auxotroph to utilize Pro-Gly as a proline source. dppA-dependent Pro-Gly utilization does not require any of the three major proline transport systems, demonstrating that DppA is not simply a dipeptidase. An in vivo competition assay was used to show that DppA is probably involved in the transport of dipeptides other than Pro-Gly. Transcription of dppA is repressed by the presence of casamino acids, suggesting that the cell alters its dipeptide transport capabilities in response to an environmental signal.

Links

PubMed PMC207180

Keywords

Amino Acid Sequence; Bacterial Proteins/genetics; Bacteriophage lambda/genetics; Base Sequence; Biological Transport; Blotting, Northern; Carrier Proteins/genetics; DNA, Bacterial/genetics; DNA, Bacterial/isolation & purification; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Genes, Bacterial; Membrane Transport Proteins/genetics; Molecular Sequence Data; Nucleic Acid Hybridization; Oligonucleotide Probes; Periplasmic Binding Proteins; Plasmids; RNA, Bacterial/genetics; RNA, Bacterial/isolation & purification; Restriction Mapping; Sequence Homology, Nucleic Acid

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