The Escherichia coli azoreductase AzoR is involved in resistance to thiol-specific stress caused by electrophilic quinones

Abstract

The physiological role of Escherichia coli azoreductase AzoR was studied. It was found that AzoR was capable of reducing several benzo-, naphtho-, and anthraquinone compounds, which were better substrates for AzoR than the model azo substrate methyl red. The ΔazoR mutant displayed reduced viability when exposed to electrophilic quinones, which are capable of depleting cellular reduced glutathione (GSH). Externally added GSH can partially restore the impaired growth of the ΔazoR mutant caused by 2-methylhydroquinone. The transcription of azoR was induced by electrophiles, including 2-methylhydroquinone, catechol, menadione, and diamide. A transcription start point was identified 44 bp upstream from the translation start point. These data indicated that AzoR is a quinone reductase providing resistance to thiol-specific stress caused by electrophilic quinones. Copyright © 2009, American Society for Microbiology. All Rights Reserved.