Genetic Organization of the Oligopeptide Permease (
 opp
 ) Locus of
 Salmonella typhimurium
 and
 Escherichia coli

Hogarth, Barbara G.; Higgins, Christopher F.

doi:10.1128/jb.153.3.1548-1551.1983

Cited by 46 publications

(12 citation statements)

References 12 publications

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“…Fifteen independent opp::Mu dl insertions (CH226 through CH229 and CH257 through CH267) were each mapped to one of the four opp genes by complementation analysis with F' opp episomes containing defined nonpolar mutations in opp, as described previously (14). At least one insertion in each of the four opp genes was obtained ( Table 1).…”

Section: Methodsmentioning

confidence: 99%

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Anaerobic and leucine-dependent expression of a peptide transport gene in Salmonella typhimurium

Jamieson¹,

Higgins²

1984

J Bacteriol

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Using Mu dl-mediated lac operon fusions, we studied the transcriptional regulation of the genes encoding two peptide transport systems, the oligopeptide permease and the tripeptide permease. The four opp genes were found to be constitutively expressed, whereas the genes encoding the tripeptide permease are under a complex set of regulatory controls. Two loci, tppA and tppB, are required for tripeptide permease function. Locus tppA is shown to be a positive regulator of tppB expression. In addition, tppB expression is specifically induced by exogenous leucine or by anaerobiosis. Anaerobic induction of tppB is independent of thefnr gene product which is required for the anaerobic expression of several respiratory enzymes. Thus, there must be at least two distinct pathways for the anaerobic regulation of gene expression. minimal medium. Kanamycin (Kan) and Chloramphenicol (Cml) were used at 25 ,ug ml-1 and 12.5 ,ug ml-l, respectively. 5-Bromo-4-chloro-3-indoyl-p-D-galactoside (Bethesda Research Laboratories) was added to LB plates at 160 Fig ml-' and to minimal plates at 20 ,ug ml-. Bacteriophage. Phage Mu does not ordinarily infect S. typhimurium. However, lysates of a strain lysogenic for both Mu dl and a Mu/P1 hybrid phage (JL3473) are able to infect P1-sensitive (i.e., galE) derivatives of S. typhimurium (5). Heat-induced lysates of JL3473 grown in LC medium were 131

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Section: Methodsmentioning

confidence: 99%

“…Opp is now relatively well characterized. This transport system is encoded by a single operon consisting of four genes, oppA, oppB, oppC, and oppD (13,14), which map near trp at 34 min on the S. typhimurium chromosomal map (34). Gene oppA encodes a periplasmic protein with a molecular weight of 52,000 (12).…”

mentioning

confidence: 99%

Anaerobic and leucine-dependent expression of a peptide transport gene in Salmonella typhimurium

Jamieson¹,

Higgins²

1984

J Bacteriol

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“…The first 13 residues of the protein were determined and found to match residues 27±39 of the oppA gene product. OppA is the periplasmic-binding protein component of the OppABCDF oligopeptide transport system (Hogarth and Higgins, 1983;Andrews and Short, 1985); synthesis of mature OppA protein includes the removal of its N-terminal leader peptide preceding residue 27 during its translocation to the periplasm (Guyer et al, 1985).…”

Section: Lysogen or Transformantmentioning

confidence: 99%

The gcvB gene encodes a small untranslated RNA involved in expression of the dipeptide and oligopeptide transport systems in Escherichia coli

Urbanowski

Stauffer

Stauffer³

2000

Molecular Microbiology

200

251

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The Escherichia coli gcvB gene encodes a small RNA transcript that is not translated in vivo. Transcription from the gcvB promoter is activated by the GcvA protein and repressed by the GcvR protein, the transcriptional regulators of the gcvTHP operon encoding the enzymes of the glycine cleavage system. A strain carrying a chromosomal deletion of gcvB exhibits normal regulation of gcvTHP expression and glycine cleavage enzyme activity. However, this mutant has high constitutive synthesis of OppA and DppA, the periplasmic‐binding protein components of the two major peptide transport systems normally repressed in cells growing in rich medium. The altered regulation of oppA and dppA was also demonstrated using oppA–phoA and dppA–lacZ gene fusions. Although the mechanism(s) involving gcvB in the repression of these two genes is not known, oppA regulation appears to be at the translational level, whereas dppA regulation occurs at the mRNA level.

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“…Nutrient accumulation is the most obvious function of these transporters, but they also play a role in biological processes such as sporulation, heme synthesis, gene expression, and chemotaxis (1)(2)(3)(4). Structurally diverse peptide transporters have been characterized, but the majority of the high-affinity systems belong to the ABC transporter superfamily (1,(5)(6)(7). These are multicomponent/domain transport systems composed of two integral membrane units and two peripheral ATP-binding units, which function together with an extracytoplasmic solute-binding protein (8).…”

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confidence: 99%

Kinetics and Structural Requirements for the Binding Protein of the Di-tripeptide Transport System of Lactococcus lactis

et al. 2000

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The gene (dppA) encoding the binding protein of the di-tripeptide ABC transporter of Lactococcus lactis (DppA) was cloned under the control of the nisin promoter. Amplified expression ( approximately 200-fold increase) of the protein fused to a carboxyl-terminal six-histidine tag allowed the purification of DppA-(His)(6) by nickel-chelate affinity and anion-exchange chromatography. Ligand binding to DppA-(His)(6) elicited an electrophoretic mobility shift, a decrease in the intrinsic fluorescence, and a blue shift of the emission maximum. Each of these parameters detected conformational changes in the protein that reflect ligand binding, and these were used to determine the structural requirements of DppA-(His)(6) for binding peptides. The major features of peptide binding include (i) high affinity for di- and tripeptides, (ii) requirement of a free N-terminal alpha-amino group and an alpha-peptide bound contiguous with the N-terminal amino group, (iii) stereospecificity for L-isomers, and (iv) preference for dipeptides containing methionine or arginine, followed by hydrophobic tripeptides consisting of leucine or valine residues. Maximal binding affinity was detected at pH 6.0, and the K(d) for binding increased 1 order of magnitude for every unit increase in pH. This suggests that the ionization of protein residues (pK > 6.0) in or in close proximity to the binding site is critical in the binding mechanism.

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Genetic Organization of the Oligopeptide Permease ( opp ) Locus of Salmonella typhimurium and Escherichia coli

Cited by 46 publications

References 12 publications

Anaerobic and leucine-dependent expression of a peptide transport gene in Salmonella typhimurium

Anaerobic and leucine-dependent expression of a peptide transport gene in Salmonella typhimurium

The gcvB gene encodes a small untranslated RNA involved in expression of the dipeptide and oligopeptide transport systems in Escherichia coli

Kinetics and Structural Requirements for the Binding Protein of the Di-tripeptide Transport System of Lactococcus lactis

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