Molecular characterization of the oligopeptide permease of Salmonella typhimurium

Hiles, Ian D.; Gallagher, Maurice P.; Jamieson, Derek J.; Higgins, Christopher F.

doi:10.1016/0022-2836(87)90332-9

Cited by 255 publications

(172 citation statements)

References 62 publications

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“…Although IS2 was observed in another polyamine-requiring mutant HT283 (EWH319), it was not in E. coli W3110, the parental strain of MA261 and HT283. The upstream region of the gene also included the leucine responsive element observed in the upstream region of the oppA gene of Salmonella typhimurium (31). We confirmed leucine stimulation of OppA synthesis in E. coli HT283, but polyamine stimulation of OppA synthesis was not influenced by leucine (data not shown).…”

Section: Polyamine Stimulation Of Oppa Synthesis Is Dependent Onsupporting

confidence: 70%

Molecular Mechanism of Polyamine Stimulation of the Synthesis of Oligopeptide-binding Protein

Igarashi

Saisho

Yuguchi

et al. 1997

Journal of Biological Chemistry

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Section: Polyamine Stimulation Of Oppa Synthesis Is Dependent Onsupporting

confidence: 70%

Molecular Mechanism of Polyamine Stimulation of the Synthesis of Oligopeptide-binding Protein

Igarashi

Saisho

Yuguchi

et al. 1997

Journal of Biological Chemistry

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“…The genetic linkage of an endopeptidase gene to the opp operon is unique for L. lactis. In the other binding-protein-dependent oligopeptide transport systems characterized (those of E. coli, Salmonella typhimunium, Bacillus subtilis, and Streptococcus pneumoniae), the gene order in the operons is mutually identical and different from that in L. lactis (1,15,16,44). In L. lactis, oppA is the last of the opp genes, whereas in the other bacteria it is the first gene of the operons.…”

Section: Resultsmentioning

confidence: 99%

“…The 127-bp region between oppA and pepO in L. lactis contains a weak rho-independent terminator. The region downstream of oppA in S. typhimurium is also followed by a long intercistronic region containing a rho-independent terminator-like structure (15), to which no function has yet been ascribed. In the deduced amino acid sequence of PepO, no typical prokaryotic signal sequence (74) was present.…”

Section: Resultsmentioning

confidence: 99%

Cloning and sequencing of the gene for a lactococcal endopeptidase, an enzyme with sequence similarity to mammalian enkephalinase

et al. 1993

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The gene specifying an endopeptidase of Lactococcus lactis, named pepO, was cloned from a genomic library of L. lactis subsp. cremoris P8-2-47 in lambda EMBL3 and was subsequently sequenced. pepO is probably the last gene of an operon encoding the binding-protein-dependent oligopeptide transport system of L. lactis. The inferred amino acid sequence of PepO showed that the lactococcal endopeptidase has a marked similarity to the mammalian neutral endopeptidase EC 3.4.24.11 (enkephalinase), whereas no obvious sequence similarity with any bacterial enzyme was found. By means of gene disruption, a pepO-negative mutant was constructed. Growth and acid production of the mutant strain in milk were not affected, indicating that the endopeptidase is not essential for growth of L. lactis in milk.

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“…TAP1 and TAP2 are thought to form a heterodimer [13,14] located in the membrane of the ER and cis-Golgi [15]. Other members of the family include the multidrug resistance P-glycoprotein (MDR) [16], the cystic fibrosis transmembrane conductance regulator (CFTR) [17], the oligopeptide transporter of Salmonella typhimurium [18] and the yeast protein Ste6 [19,20]. *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells

et al. 1994

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Using the baculovirus expression system the gene products of human tapl and tap2 were over-expressed as wild-type as well as oligohistidine fusion proteins in Spodopterafrugiperda (Sf9) insect cells, Both gene products were co-expressed within the same cells and were found enriched in microsomal membranes. Immunoprecipitation and immobilized metal affinity chromatography revealed complex formation between TAP1 and TAP2. The expressed TAP complex was shown to be functional by peptide translocation into microsomes of Sf9 cells. Peptide transport strictly requires TAP1 and TAP2 as well as ATE For the first time the functional expression ofthe human TAP complex in insect cells has been demonstrated, indicating that additional cofactors of a highly developed immune system are not essential for peptide transport across microsomal membranes.

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Molecular characterization of the oligopeptide permease of Salmonella typhimurium

Cited by 255 publications

References 62 publications

Molecular Mechanism of Polyamine Stimulation of the Synthesis of Oligopeptide-binding Protein

Molecular Mechanism of Polyamine Stimulation of the Synthesis of Oligopeptide-binding Protein

Cloning and sequencing of the gene for a lactococcal endopeptidase, an enzyme with sequence similarity to mammalian enkephalinase

Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells

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