1887

Abstract

The σ RNA polymerase subunit has a prominent role in susceptibility of and to mesentericin Y105, a class IIa bacteriocin. Consequently, σ-dependent genes as well as specific activators also required for expression of these genes were sought. Five putative σ-associated activators were detected in the genome of V583, and all but one could activate the transcription of permease genes belonging to sugar phosphotransferase systems (PTSs). Interestingly, these activators display a helicase signature not yet reported in this activator family, which could explain the ATP-dependent mechanism of DNA unwinding preceding the start of transcription. To find which activator is linked to susceptibility of to mesentericin Y105, their respective genes were subsequently interrupted. Among them, only gene interruption led to a resistance phenotype. Immediately downstream from , a putative σ-dependent operon was found to encode a mannose PTS permease, namely \(EII_{t}^{Man}\) . Moreover, in liquid culture, glucose and mannose induced the sensitivity of to mesentericin Y105. Since sugars have previously been reported to induce PTS permease expression, it appears that \(EII_{t}^{Man}\) expression, presumably induced in the presence of glucose and mannose, leads to an enhanced sensitivity of to the bacteriocin. Additional information was gained from knockouts within the permease operon. Interruption of the distal gene, which encodes the IID subunit of \(EII_{t}^{Man}\) , strikingly led to resistance to mesentericin Y105. Moreover, MptD appears to be a peculiar membrane subunit, bearing an additional domain compared to most known IID subunits. According to these results, \(EII_{t}^{Man}\) is clearly involved in susceptibility to mesentericin Y105 and could even be its receptor at the surface. Finally, it is hypothesized that MptD could be responsible for the targeting specificity, via an interaction between its additional domain and mesentericin Y105.

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2001-06-01
2019-10-18
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