1887

Abstract

The ability of pv. to protect itself against lethal concentrations of man-made (-ethylmaleimide, NEM) and endogenously produced (methylglyoxal, MG) electrophiles was investigated. Pretreatment of . pv. with a low concentration of NEM induced protection against lethal concentrations of NEM and MG. MG pretreatment weakly induced protection against NEM but not against MG itself. NEM-induced protection against electrophile killing required new protein synthesis and was abolished by the addition of a protein synthesis inhibitor. By contrast, MG-induced protection against NEM killing was independent of protein synthesis. . pv. harbouring an expression vector carrying a catalase gene was over 100-fold more resistant to MG and NEM killing. High expression levels of genes for other peroxide-protective enzymes, such as those for alkyl hydroperoxide reductase ( and ) and , failed to protect against electrophile killing. Thus, catalase appears to have a novel protective role(s) against electrophile toxicity. This finding suggests that in . pv. NEM and MG toxicity might involve accumulation and/or increased production of HO. This idea was supported by the observation that addition of 10 mM sodium pyruvate, a compound that can react chemically with peroxide or hydroxyl radical scavengers (DMSO and glycerol), was found to protect from electrophile killing. The protective role of catalase and the role of HO in electrophile toxicity are novel observations and could be generally important in other bacteria. In addition, unlike other bacteria, in stationary phase was more susceptible to electrophile killing compared to cells in exponential phase.

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2001-02-01
2021-07-27
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