Redox-operated genetic switches: the SoxR and OxyR transcription factors

• Published in: Trends in Biotechnology Vol. 19; no. 3; pp. 109 - 114
• Main Authors: Pomposiello, Pablo J, Demple, Bruce
• Format: Book Review Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01-03-2001; Elsevier Science
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacteriology; Biological and medical sciences; Biotechnology; Disulfides - chemistry; DNA-Binding Proteins; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins; Free Radicals - metabolism; Fundamental and applied biological sciences. Psychology; Genetic engineering; Genetic technics; Genetics; hydrogen peroxide; Hydrogen Peroxide - metabolism; iron-sulphur clusters; Methods. Procedures. Technologies; Microbiology; Miscellaneous; nitric oxide; Nitric Oxide - metabolism; Oxidation-Reduction; oxidative stress; OxyR; OxyR protein; redox sensing; Repressor Proteins - chemistry; Repressor Proteins - genetics; Repressor Proteins - metabolism; SoxR; SoxR protein; superoxide; Superoxides - metabolism; Synthetic digonucleotides and genes. Sequencing; transcription factors; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism; Transcriptional Activation; SoxR; nitric oxide; redox sensing; transcription factors; OxyR; hydrogen peroxide; iron-sulphur clusters; superoxide; oxidative stress; Oxidative stress; Regulation(control); Redox potential; Gene expression; Application; Hydrogen Peroxides; Free radical
• ISSN: 0167-7799; 1879-3096
• DOI: 10.1016/S0167-7799(00)01542-0

Two redox-responsive transcription regulators have been well defined in
Escherichia coli and serve as paradigms of redox-operated genetic switches. SoxR contains iron–sulfur centers that activate the protein when they are one-electron oxidized, or nitrosylated by nitric oxide. OxyR contains a pair of redox-active cysteine residues that activate the protein when they are oxidized to form a disulfide bond.