The Escherichia coli Azoreductase AzoR Is Involved in Resistance to Thiol-Specific Stress Caused by Electrophilic Quinones
Author(s) -
Guangfei Liu,
Jiti Zhou,
Qi Fu,
Jing Wang
Publication year - 2009
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.00552-09
Subject(s) - menadione , biology , escherichia coli , glutathione , electrophile , biochemistry , quinone , glutathione reductase , thiol , mutant , reductase , oxidative stress , enzyme , gene , glutathione peroxidase , catalysis
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 DeltaazoR 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 DeltaazoR 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.
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