Peroxide-Sensing Transcriptional Regulators in Bacteria
- 15 October 2012
- journal article
- review article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 194 (20), 5495-5503
- https://doi.org/10.1128/jb.00304-12
Abstract
The ability to maintain intracellular concentrations of toxic reactive oxygen species (ROS) within safe limits is essential for all aerobic life forms. In bacteria, as well as other organisms, ROS are produced during the normal course of aerobic metabolism, necessitating the constitutive expression of ROS scavenging systems. However, bacteria can also experience transient high-level exposure to ROS derived either from external sources, such as the host defense response, or as a secondary effect of other seemingly unrelated environmental stresses. Consequently, transcriptional regulators have evolved to sense the levels of ROS and coordinate the appropriate oxidative stress response. Three well-studied examples of these are the peroxide responsive regulators OxyR, PerR, and OhrR. OxyR and PerR are sensors of primarily H 2 O 2 , while OhrR senses organic peroxide (ROOH) and sodium hypochlorite (NaOCl). OxyR and OhrR sense oxidants by means of the reversible oxidation of specific cysteine residues. In contrast, PerR senses H 2 O 2 via the Fe-catalyzed oxidation of histidine residues. These transcription regulators also influence complex biological phenomena, such as biofilm formation, the evasion of host immune responses, and antibiotic resistance via the direct regulation of specific proteins.Keywords
This publication has 124 references indexed in Scilit:
- S-Bacillithiolation Protects Against Hypochlorite Stress in Bacillus subtilis as Revealed by Transcriptomics and Redox ProteomicsMolecular & Cellular Proteomics, 2011
- Differential Secretomics of Streptococcus pyogenes Reveals a Novel Peroxide Regulator (PerR)-regulated Extracellular Virulence Factor Mitogen Factor3 (MF3)Molecular & Cellular Proteomics, 2011
- Thiol-Based Redox Switches and Gene RegulationAntioxidants and Redox Signaling, 2011
- Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganeseProceedings of the National Academy of Sciences of the United States of America, 2011
- Oral-Derived Bacterial Flora Defends Its Domain by Recognizing and Killing Intruders—A Molecular Analysis Using Escherichia coli as a Model Intestinal BacteriumMicrobial Ecology, 2010
- Ohr (Organic Hydroperoxide Resistance Protein) Possesses a Previously Undescribed Activity, Lipoyl-dependent PeroxidaseJournal of Biological Chemistry, 2010
- Crystal Structures of the Reduced, Sulfenic Acid, and Mixed Disulfide Forms of SarZ, a Redox Active Global Regulator in Staphylococcus aureusJournal of Biological Chemistry, 2009
- Polymicrobial interactions stimulate resistance to host innate immunity through metabolite perceptionProceedings of the National Academy of Sciences of the United States of America, 2009
- Cytotoxicity of Pseudomonas Secreted Exotoxins Requires OxyR ExpressionJournal of Surgical Research, 2007
- A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrRProceedings of the National Academy of Sciences of the United States of America, 2007