Oligopeptide Binding Protein Oppa
Mostrando 1-12 de 17 artigos, teses e dissertações.
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1. Distribution and biological role of the oligopeptide-binding protein (OppA) in Xanthomonas species
In this study we investigated the prevalence of the oppA gene, encoding the oligopeptide binding protein (OppA) of the major bacterial oligopeptide uptake system (Opp), in different species of the genus Xanthomonas. The oppA gene was detected in two Xanthomonas axonopodis strains among eight tested Xanthomonas species. The generation of an isogenic oppA-knoc
Genetics and Molecular Biology. Publicado em: 07/06/2010
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2. Estudo do transporte de oligopeptídeos em Aeromonas hydrophila e comparação com outras espécies do gênero
O sistema de transporte de oligopeptídios (sistema Opp) está envolvido em diferentes aspectos da fisiologia bacteriana, incluindo nutrição, comunicação intercelular e fatores associados com a virulência. Estes transportadores ABC são formados por uma proteína de ligação a oligopeptídios, uma permease e um domínio de ligação ao ATP. As Aeromona
Publicado em: 2008
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3. Intracellular polyamine pools, oligopeptide-binding protein A expression, and resistance to aminoglycosides in Escherichia coli
The role of intracellular free polyamine (putrescine and spermidine) pools in multiple resistance to aminoglycoside antibiotics was investigated among in vitro selected kanamycin-resistant Escherichia coli J53 mutants expressing diminished oligopeptide-binding protein (OppA) levels and/or defective ornithine decarboxylase (ODC) activity. The results suggest
Memórias do Instituto Oswaldo Cruz. Publicado em: 2005-11
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4. Increase of sensitivity to aminoglycoside antibiotics by polyamine-induced protein (oligopeptide-binding protein) in Escherichia coli.
The sensitivity of Escherichia coli to several aminoglycoside antibiotics was examined with E. coli DR112 transformed by the gene for polyamine-induced protein (oligopeptide-binding [OppA] protein) or polyamine transport proteins. The results clearly showed that sensitivity to aminoglycoside antibiotics (gentamicin, isepamicin, kanamycin, neomycin, paromomyc
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5. Specificity Mutants of the Binding Protein of the Oligopeptide Transport System of Lactococcus lactis
The kinetic properties of wild-type and mutant oligopeptide binding proteins of Lactococcus lactis were determined. To observe the properties of the mutant proteins in vivo, the oppA gene was deleted from the chromosome of L. lactis to produce a strain that was totally defective in oligopeptide transport. Amplified expression of the oppA gene resulted in an
American Society for Microbiology.
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6. OppA of Listeria monocytogenes, an Oligopeptide-Binding Protein Required for Bacterial Growth at Low Temperature and Involved in Intracellular Survival
We identified a new oligopeptide permease operon in the pathogen Listeria monocytogenes. This opp operon consists of five genes (oppA, oppB, oppC, oppD, and oppF) and displays the same genetic organization as those of several bacterial species. The first gene of this operon, oppA, encodes a 62-kDa protein sharing 33% identity with OppA of Bacillus subtilis a
American Society for Microbiology.
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7. OppA, the Substrate-Binding Subunit of the Oligopeptide Permease, Is the Major Ecto-ATPase of Mycoplasma hominis
Most ATPases, involved in energy-driven processes, act in the cytoplasm. However, external membrane-bound ATPases have also been described in parasites and eukaryotic cells. In Mycoplasma hominis, a bacterium lacking a cell wall, the surface-exposed substrate-binding protein OppA of an oligopeptide permease (Opp) contains an ATP binding P-loop structure in t
American Society for Microbiology.
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8. Relationship between Spontaneous Aminoglycoside Resistance in Escherichia coli and a Decrease in Oligopeptide Binding Protein
Changes in the amount of oligopeptide binding protein (OppA) in spontaneous kanamycin-resistant mutants of Escherichia coli were investigated. Among 20 colonies obtained from 108 cells cultured in the presence of 20 μg of kanamycin/ml, 1 colony had no detectable OppA and 7 colonies were mutants with reduced amounts of OppA. Sensitivity of wild-type cells to
American Society for Microbiology.
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9. Identification of a Differentially Expressed Oligopeptide Binding Protein (OppA2) in Streptococcus uberis by Representational Difference Analysis of cDNA
Streptococcus uberis is an increasingly significant cause of intramammary infection in the dairy cow, presently responsible for approximately 33% of all cases of bovine mastitis in the United Kingdom. Following experimentally induced infection of the lactating mammary gland, S. uberis is found predominantly in the luminal areas of secretory alveoli and ductu
American Society for Microbiology.
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10. Combinatorial peptide libraries reveal the ligand-binding mechanism of the oligopeptide receptor OppA of Lactococcus lactis
The oligopeptide transport system (Opp) of Lactococcus lactis has the unique capacity to mediate the transport of peptides from 4 up to at least 18 residues. The substrate specificity of this binding protein-dependent ATP-binding cassette transporter is determined mainly by the receptor protein OppA. To study the specificity and ligand-binding mechanism
The National Academy of Sciences.
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11. Analysis of Differences in the Functional Properties of the Substrate Binding Proteins of the Borrelia burgdorferi Oligopeptide Permease (opp) Operon
The Borrelia burgdorferi genome encodes five orthologues of the substrate binding protein oligopeptide permease A (OppA). It was previously shown that these genes are under the control of separate promoters and are differentially expressed under various environmental conditions. We were interested in determining whether there are also differences in substrat
American Society for Microbiology.
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12. Relevance of Peptide Uptake Systems to the Physiology and Virulence of Streptococcus agalactiae
Streptococcus agalactiae is a major cause of invasive infections in human newborns. To satisfy its growth requirements, S. agalactiae takes up 9 of the 20 proteinogenic amino acids from the environment. Defined S. agalactiae mutants in one or several of four putative peptide permease systems were constructed and tested for peptide uptake, growth in various m
American Society for Microbiology.