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The Escherichia coli Azoreductase AzoR Is Involved in Resistance to Thiol-Specific Stress Caused by Electrophilic Quinones

The Escherichia coli Azoreductase AzoR Is Involved in Resistance to Thiol-Specific Stress Caused... The Escherichia coli Azoreductase AzoR Is Involved in Resistance to Thiol-Specific Stress Caused by Electrophilic Quinones ▿ Guangfei Liu 1 , Jiti Zhou 1 , Q. Shiang Fu 1 , 2 , 3 , and Jing Wang 1 , * 1 Key Laboratory of Industrial Ecology and Environmental Engineering, Ministry of Education, School of Environmental and Biological Science and Technology, Dalian University of Technology, Dalian 116024, China 2 Department of Civil and Environmental Engineering, Stanford University, Stanford, California 94305-4020 3 Nanjing Institute of Geography and Limnology, Chinese Academy of Sciences, Nanjing, China 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Bacteriology American Society For Microbiology

The Escherichia coli Azoreductase AzoR Is Involved in Resistance to Thiol-Specific Stress Caused by Electrophilic Quinones

Journal of Bacteriology , Volume 191 (20): 6394 – Oct 15, 2009

The Escherichia coli Azoreductase AzoR Is Involved in Resistance to Thiol-Specific Stress Caused by Electrophilic Quinones

Journal of Bacteriology , Volume 191 (20): 6394 – Oct 15, 2009

Abstract

The Escherichia coli Azoreductase AzoR Is Involved in Resistance to Thiol-Specific Stress Caused by Electrophilic Quinones ▿ Guangfei Liu 1 , Jiti Zhou 1 , Q. Shiang Fu 1 , 2 , 3 , and Jing Wang 1 , * 1 Key Laboratory of Industrial Ecology and Environmental Engineering, Ministry of Education, School of Environmental and Biological Science and Technology, Dalian University of Technology, Dalian 116024, China 2 Department of Civil and Environmental Engineering, Stanford University, Stanford, California 94305-4020 3 Nanjing Institute of Geography and Limnology, Chinese Academy of Sciences, Nanjing, China 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.

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References (51)

Publisher
American Society For Microbiology
Copyright
Copyright © 2009 by the American society for Microbiology.
ISSN
0021-9193
eISSN
1098-5530
DOI
10.1128/JB.00552-09
pmid
19666717
Publisher site
See Article on Publisher Site

Abstract

The Escherichia coli Azoreductase AzoR Is Involved in Resistance to Thiol-Specific Stress Caused by Electrophilic Quinones ▿ Guangfei Liu 1 , Jiti Zhou 1 , Q. Shiang Fu 1 , 2 , 3 , and Jing Wang 1 , * 1 Key Laboratory of Industrial Ecology and Environmental Engineering, Ministry of Education, School of Environmental and Biological Science and Technology, Dalian University of Technology, Dalian 116024, China 2 Department of Civil and Environmental Engineering, Stanford University, Stanford, California 94305-4020 3 Nanjing Institute of Geography and Limnology, Chinese Academy of Sciences, Nanjing, China 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.

Journal

Journal of BacteriologyAmerican Society For Microbiology

Published: Oct 15, 2009

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