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Distribution and biological role of the oligopeptide-binding protein (OppA) in Xanthomonas species Genet. Mol. Biol.
Oshiro,Elisa E.; Tavares,Milene B.; Suzuki,Celso F.; Pimenta,Daniel C.; Angeli,Claudia B.; Oliveira,Julio C.F. de; Ferro,Maria I.T.; Ferreira,Luis C.S.; Ferreira,Rita C.C..
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-knockout derivative of the Xac 306 strain, showed that the OppA protein neither plays a relevant role in oligopeptide uptake nor contributes to the infectivity and multiplication of the bacterial strain in leaves of sweet orange (Citrus sinensis) and Rangpur lime (Citrus limonia). Taken together these results suggest that the oppA gene has a recent evolutionary history in the genus and does not contribute...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Xanthomonas; Xac; OppA; Oligopeptide uptake system; ABC transporter.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572010000200023
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Effect of sigma factor S (sigmaS) on the stability of penicillin-binding protein 3 (PBP3) of Escherichia colt K12 Braz. J. Genet.
Machado,Rosane S.; Camelo,Douglas C.; Almeida,Darcy F. de; Ferreira,Luis C.S..
The stability of penicillin-binding protein 3 (PBP3), a cell septum synthesizing protein, was analyzed at different incubation temperatures in three Escherichia coli K12 strains carrying a PBP3-overproducing plasmid. The stability of PBP3 was significantly reduced in stationary phase cells shifted to 42°C for 4 h, compared to samples incubated at 28 or 37°C. The half-life of PBP3 in the C600 strain was 60 min at 42°C, while samples incubated at 28 or 37°C had PBP3 half-lives greater than 4 h. Analysis of the PBP3 content in mutants deficient in rpoS (coding for the stationary phase sigma factor, sigmaS) and rpoH (coding for the heat shock sigma factor, sigma32) genes after shift to 42°C showed that stability of the protein was controlled by sigmaS but not...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Sigma factor S; Penicillin-binding protein; Escherichia colt K12.
Ano: 1996 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-84551996000400001
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