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Id: lil-716304
Autor: Riboldi, Gustavo Pelicioli; Bierhals, Christine Garcia; Mattos, Eduardo Preusser de; Frazzon, Ana Paula Guedes; d?Azevedo, Pedro Alves; Frazzon, Jeverson.
Título: Oxidative stress enhances the expression of sulfur assimilation genes: preliminary insights on the Enterococcus faecalis iron-sulfur cluster machinery regulation
Fonte: Mem. Inst. Oswaldo Cruz;109(4):408-413, 03/07/2014. graf.
Idioma: en.
Projeto: CNPq; . CNPq; . CNPq; . CAPES.
Resumo: The Firmicutes bacteria participate extensively in virulence and pathological processes. Enterococcus faecalis is a commensal microorganism; however, it is also a pathogenic bacterium mainly associated with nosocomial infections in immunocompromised patients. Iron-sulfur [Fe-S] clusters are inorganic prosthetic groups involved in diverse biological processes, whose in vivo formation requires several specific protein machineries. Escherichia coli is one of the most frequently studied microorganisms regarding [Fe-S] cluster biogenesis and encodes the iron-sulfur cluster and sulfur assimilation systems. In Firmicutes species, a unique operon composed of the sufCDSUB genes is responsible for [Fe-S] cluster biogenesis. The aim of this study was to investigate the potential of the E. faecalis sufCDSUB system in the [Fe-S] cluster assembly using oxidative stress and iron depletion as adverse growth conditions. Quantitative real-time polymerase chain reaction demonstrated, for the first time, that Gram-positive bacteria possess an OxyR component responsive to oxidative stress conditions, as fully described for E. coli models. Likewise, strong expression of the sufCDSUB genes was observed in low concentrations of hydrogen peroxide, indicating that the lowest concentration of oxygen free radicals inside cells, known to be highly damaging to [Fe-S] clusters, is sufficient to trigger the transcriptional machinery for prompt replacement of [Fe-S] clusters.
Descritores: Enterococcus faecalis/metabolismo
Proteínas Ferro-Enxofre/genética
Estresse Oxidativo
-Vias Biossintéticas
Proteínas Ferro-Enxofre/biossíntese
Modelos Moleculares
Reação em Cadeia da Polimerase em Tempo Real
Especificidade por Substrato
Responsável: BR1.1 - BIREME



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