Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria

Chiang, Sarah M.; Schellhorn, Herb E.

doi:10.1016/j.abb.2012.02.007

Cited by 383Bacterial Genetics and BiotechnologyRedox biology and oxidative stressEscherichia coli research studies

Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria

Chiang, Sarah M., Schellhorn, Herb E.·2012·Archives of Biochemistry and Biophysics

DOI 10.1016/j.abb.2012.02.007

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Abstract

Oxidative stress, through the production of reactive oxygen species, is a natural consequence of aerobic metabolism. Escherichia coli has several major regulators activated during oxidative stress, including OxyR, SoxRS, and RpoS. OxyR and SoxR undergo conformation changes when oxidized in the presence of hydrogen peroxide and superoxide radicals, respectively, and subsequently control the expression of cognate genes. In contrast, the RpoS regulon is induced by an increase in RpoS levels. Current knowledge regarding the activation and function of these regulators and their dependent genes in E. coli during oxidative stress forms the scope of this review. Despite the enormous genomic diversity of bacteria, oxidative stress response regulators in E. coli are functionally conserved in a wide range of bacterial groups, possibly reflecting positive selection of these regulators. SoxRS and RpoS homologs are present and respond to oxidative stress in Proteobacteria, and OxyR homologs are present and function in H(2)O(2) resistance in a range of bacteria, from gammaproteobacteria to Actinobacteria. Bacteria have developed complex, adapted gene regulatory responses to oxidative stress, perhaps due to the prevalence of reactive oxygen species produced endogenously through metabolism or due to the necessity of aerotolerance mechanisms in anaerobic bacteria exposed to oxygen.

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ROS response is under the control of master regulators and transcription factors such as OxyR, PerR, OhrR, and SoxRS, which can be stimulated by direct oxidation of their sensor proteins and then regulate the bacterial comeback appropriately.
“can be stimulated by direct oxidation of their sensor proteins and then regulating the bacterial comeback appropriately [192].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [192]

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OxyR Regulon Controls Lipid Peroxidation-mediated Oxidative Stress in Escherichia coli
Yoon, S.-J., Park, J.-E., Yang, J.-H., & Park, J. (2002) · BMB Reports · doi:10.5483/bmbrep.2002.35.3.297 · Cited by 44 · see citing works
Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli
Liochev, S. I., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31509-6 · Cited by 42 · see citing works
Regulation of the katG‐dpsA operon and the importance of KatG in survival of Burkholderia pseudomallei exposed to oxidative stress
Loprasert, S., Whangsuk, W., Sallabhan, R., & Mongkolsuk, S. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00328-4 · Cited by 41 · see citing works
Role of the Stationary Growth Phase Sigma Factor RpoS of Burkholderia pseudomallei in Response to Physiological Stress Conditions
Subsin, B., Thomas, M. S., Katzenmeier, G., Shaw, J. G., Tungpradabkul, S., & Kunakorn, M. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.23.7008-7014.2003 · Cited by 40 · see citing works
Essential roles of core starvation‐stress response loci in carbon‐starvation‐inducible cross‐resistance and hydrogen peroxide‐inducible adaptive resistance to oxidative challenge in Salmonella typhimurium
Seymour, R. L., MISHRA, P. V., Khan, M. A., & Spector, M. P. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.5451068.x · Cited by 40 · see citing works
A shared mechanism of SoxR activation by redox‐cycling compounds
Dietrich, L. E. P., & Kiley, P. J. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07552.x · Cited by 39 · see citing works
Identification of Gene Products Involved in the Oxidative Stress Response of Moraxella catarrhalis
Hoopman, T. C., Liu, W., Joslin, S. N., Pybus, C. A., Brautigam, C. A., & Hansen, E. J. (2010) · Infection and Immunity · doi:10.1128/iai.01060-10 · Cited by 39 · see citing works
DpsA protects the human pathogen Burkholderia pseudomallei against organic hydroperoxide
Loprasert, S., Whangsuk, W., Sallabhan, R., & Mongkolsuk, S. (2004) · Archives of Microbiology · doi:10.1007/s00203-004-0694-0 · Cited by 37 · see citing works
An Ortholog of OxyR in Legionella pneumophila Is Expressed Postexponentially and Negatively Regulates the Alkyl Hydroperoxide Reductase ( ahpC2D ) Operon
LeBlanc, J. J., Brassinga, A. K. C., Ewann, F., Davidson, R., & Hoffman, P. S. (2008) · Journal of Bacteriology · doi:10.1128/jb.00141-08 · Cited by 36 · see citing works
Molecular and Physiological Effects of Mycobacterial oxyR Inactivation
Pagán-Ramos, E., Master, S. S., Pritchett, C. L., Reimschuessel, R., Trucksis, M., Timmins, G. S., & Deretic, V. P. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.7.2674-2680.2006 · Cited by 36 · see citing works
DRA0336, another OxyR homolog, involved in the antioxidation mechanisms in Deinococcus radiodurans
Yin, L., Wang, L., Lu, H., Xu, G., Chen, H., Zhan, H., Tian, B., & Hua, Y. (2010) · The Journal of Microbiology · doi:10.1007/s12275-010-0043-8 · Cited by 30 · see citing works
Identification of Brucella abortus OxyR and Its Role in Control of Catalase Expression
Kim, J., & Mayfield, J. E. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.19.5631-5633.2000 · Cited by 29 · see citing works
The RpoS Sigma Factor in the Dissimilatory Fe(III)-Reducing Bacterium Geobacter sulfurreducens
Núñez, C. E., Adams, L. A., Childers, S. E., & Lovley, D. R. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.16.5543-5546.2004 · Cited by 29 · see citing works
Induction of peroxide and superoxide protective enzymes and physiological cross-protection against peroxide killing by a superoxide generator inVibrio harveyi
Vattanaviboon, P., Panmanee, W., & Mongkolsuk, S. (2003) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(03)00172-1 · Cited by 28 · see citing works
Role of oxyR from Sinorhizobium meliloti in Regulating the Expression of Catalases
Luo, L., Qi, M., Yao, S., Cheng, H., Zhu, J., & Yu, G. (2005) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2005.00055.x · Cited by 27 · see citing works
The structure of a reduced form of OxyR from Neisseria meningitidis
Sainsbury, S., Ren, J., Nettleship, J. E., Saunders, N. J. S. G., Stuart, D. I., & Owens, R. J. (2010) · BMC Structural Biology · doi:10.1186/1472-6807-10-10 · Cited by 26 · see citing works
Agrobacterium tumefaciens soxR Is Involved in Superoxide Stress Protection and Also Directly Regulates Superoxide-Inducible Expression of Itself and a Target Gene
Eiamphungporn, W., Charoenlap, N., Vattanaviboon, P., & Mongkolsuk, S. (2006) · Journal of Bacteriology · doi:10.1128/jb.00856-06 · Cited by 24 · see citing works
Genetic and physiological analysis of the major OxyR-regulated katA from Xanthomonas campestris pv. phaseoli
Chauvatcharin, N., Atichartpongkul, S., Utamapongchai, S., Whangsuk, W., Vattanaviboon, P., & Mongkolsuk, S. (2005) · Microbiology · doi:10.1099/mic.0.27598-0 · Cited by 24 · see citing works
Competitiveness in root colonization by Pseudomonas putida requires the rpoS gene
Miller, C., Kim, Y., & Anderson, A. J. (2001) · Canadian Journal of Microbiology · doi:10.1139/w00-123 · Cited by 23 · see citing works
Burkholderia pseudomallei RpoS regulates OxyR and the katG-dpsA operon under conditions of oxidative stress
Jangiam, W., Loprasert, S., Smith, D. R., & Tungpradabkul, S. (2010) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2010.00230.x · Cited by 22 · see citing works
Physiological and Regulatory Characterization of KatA and KatY in Yersinia pestis
Han, Y., Geng, J., Qiu, Y., Guo, Z., Zhou, D., Bi, Y., Du, Z., Song, Y., Wang, X., Tan, Y., et al. (2008) · DNA and Cell Biology · doi:10.1089/dna.2007.0657 · Cited by 21 · see citing works
Elevated Mutation Frequency in Surviving Populations of Carbon-Starved rpoS -Deficient Pseudomonas putida Is Caused by Reduced Expression of Superoxide Dismutase and Catalase
Tarassova, K., Tegova, R., Tover, A., Teras, R., Tark‐Dame, M., Saumaa, S., & Kivisaar, M. (2009) · Journal of Bacteriology · doi:10.1128/jb.01803-08 · Cited by 17 · see citing works
Is superoxide able to induce SoxRS?
Liochev, S. I., & Fridovich, I. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.029 · Cited by 16 · see citing works
Hydrogen Peroxide Resistance ofAcetobacter pasteurianusNBRC3283 and Its Relationship to Acetic Acid Fermentation
Okamoto-Kainuma, A., EHATA, Y., Ikeda, M., OSONO, T., Ishikawa, M., Kaga, T., & KOIZUMI, Y. (2008) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.80136 · Cited by 16 · see citing works
Mutual Regulation of Crl and Fur in Escherichia coli W3110
Lelong, C., Rolland, M., Louwagie, M., Garin, J., & Geiselmann, J. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600192-mcp200 · Cited by 11 · see citing works
Competitiveness in root colonization by Pseudomonas putida requires the rpoS gene
Miller, C., Kim, Y., & Anderson, A. J. (2001) · Canadian Journal of Microbiology · doi:10.1139/cjm-47-1-41 · Cited by 10 · see citing works
Growth of Escherichia coli in Iron-enriched Medium Increases HPI Catalase Activity
Zaid, T., Srikumar, T. S. N., & Benov, L. (2003) · BMB Reports · doi:10.5483/bmbrep.2003.36.6.608 · Cited by 8 · see citing works

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Antimicrobial strategies centered around reactive oxygen species – bactericidal antibiotics, photodynamic therapy, and beyond
Vatansever, F., Melo, W., Avci, P., Vecchio, D., Sadasivam, M., Gupta, A., Chandran, R., Karimi, M., Parizotto, N. A., Yin, R., et al. (2013) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12026 · Cited by 1,134 · see citing works
Antibiotics induce redox-related physiological alterations as part of their lethality
Dwyer, D. J., Belenky, P. A., Yang, J. H., MacDonald, I. C., Martell, J. D., Takahashi, N. K., Chan, C. T. Y., Lobritz, M. A., Braff, D., Schwarz, E. G., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401876111 · Cited by 938 · see citing works
Remaining mysteries of molecular biology: the role of polyamines in the cell
Miller-Fleming, L., Olin-Sandoval, V., Campbell, K., & Ralser, M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.06.020 · Cited by 658 · see citing works
Genome-wide mapping of mutations at single-nucleotide resolution for protein, metabolic and genome engineering
Garst, A. D., Bassalo, M. C., Pines, G., Lynch, S. A., Halweg‐Edwards, A. L., Liu, R., Liang, L., Wang, Z., Zeitoun, R. I., Alexander, W. G., et al. (2016) · Nature Biotechnology · doi:10.1038/nbt.3718 · Cited by 356 · see citing works
The Crosstalk between the Gut Microbiota and Mitochondria during Exercise
Clark, A. P., & Mach, N. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00319 · Cited by 338 · see citing works
Reactive Oxygen Species (ROS)-Mediated Antibacterial Oxidative Therapies: Available Methods to Generate ROS and a Novel Option Proposal
Alfei, S., Schito, G. C., Schito, A. M., & Zuccari, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137182 · Cited by 316 · see citing works
Reactive oxygen species in pathogen clearance: The killing mechanisms, the adaption response, and the side effects
Li, H., Zhou, X., Huang, Y., Liao, B., Cheng, L., & Ren, B. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.622534 · Cited by 284 · see citing works
Bacterial Response to Oxidative Stress and RNA Oxidation
Seixas, A. F., Quendera, A. P., Sousa, J. P. A., Silva, A. F. Q., Arraiano, C. M., & Andrade, J. M. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2021.821535 · Cited by 266 · see citing works
Genome-wide Reconstruction of OxyR and SoxRS Transcriptional Regulatory Networks under Oxidative Stress in Escherichia coli K-12 MG1655
Seo, S. W., Kim, D., Szubin, R., & Palsson, B. O. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.043 · Cited by 237 · see citing works
Copper tolerance in bacteria requires the activation of multiple accessory pathways
Giachino, A., & Waldron, K. J. (2020) · Molecular Microbiology · doi:10.1111/mmi.14522 · Cited by 223 · see citing works
Cytotoxic Cells Kill Intracellular Bacteria through Granulysin-Mediated Delivery of Granzymes
Walch, M., Dotiwala, F., Mulik, S., Thiery, J., Kirchhausen, T. L., Clayberger, C., Krensky, A. M., Martinvalet, D., & Lieberman, J. (2014) · Cell · doi:10.1016/j.cell.2014.03.062 · Cited by 223 · see citing works
Bacterial Stress Responses as Potential Targets in Overcoming Antibiotic Resistance
Dawan, J., & Ahn, J. (2022) · Microorganisms · doi:10.3390/microorganisms10071385 · Cited by 219 · see citing works
Defining Gene-Phenotype Relationships in Acinetobacter baumannii through One-Step Chromosomal Gene Inactivation
Tucker, A. T., Nowicki, E. M., Boll, J. M., Knauf, G. A., Burdis, N. C., Trent, M. S., & Davies, B. W. (2014) · mBio · doi:10.1128/mbio.01313-14 · Cited by 199 · see citing works
CodY Regulates Thiol Peroxidase Expression as Part of the Pneumococcal Defense Mechanism against H2O2 Stress
Hajaj, B., Yeşilkaya, H., Shafeeq, S., Zhi, X., Benisty, R., Shiran, T., Kuipers, O. P., & Porat, N. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00210 · Cited by 203 · see citing works
Reversible Cysteine Oxidation in Hydrogen Peroxide Sensing and Signal Transduction
García‐Santamarina, S., Boronat, S., & Hidalgo, E. (2014) · Biochemistry · doi:10.1021/bi401700f · Cited by 174 · see citing works
Thiol-based redox switches in prokaryotes
Hillion, M., & Antelmann, H. (2015) · Biological Chemistry · doi:10.1515/hsz-2015-0102 · Cited by 173 · see citing works
The DNA-Binding Protein from Starved Cells (Dps) Utilizes Dual Functions To Defend Cells against Multiple Stresses
Karas, V. O., Westerlaken, I., & Meyer, A. S. (2015) · Journal of Bacteriology · doi:10.1128/jb.00475-15 · Cited by 157 · see citing works
Alterations in human milk leptin and insulin are associated with early changes in the infant intestinal microbiome
Lemas, D. J., Young, B. E., Baker, P. R., Tomczik, A., Soderborg, T. K., Hernandez, T. L., de la Houssaye, B. A., Robertson, C. E., Rudolph, M. C., Ir, D., et al. (2016) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.115.126375 · Cited by 150 · see citing works
Fe–S proteins that regulate gene expression
Mettert, E. L., & Kiley, P. J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.11.018 · Cited by 144 · see citing works
Distribution of reactive oxygen species defense mechanisms across domain bacteria
Johnson, L. A., & Hug, L. A. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.03.032 · Cited by 143 · see citing works
The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142 · see citing works
Type VI secretion system contributes to Enterohemorrhagic Escherichia coli virulence by secreting catalase against host reactive oxygen species (ROS)
Wan, B., Zhang, Q., Ni, J., Li, S., Wen, D., Li, J., Xiao, H., He, P., Ou, H., Tao, J., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006246 · Cited by 132 · see citing works
SoxR as a Single-Cell Biosensor for NADPH-Consuming Enzymes in Escherichia coli
Siedler, S., Schendzielorz, G., Binder, S., Eggeling, L., Bringer, S., & Bott, M. H. (2013) · ACS Synthetic Biology · doi:10.1021/sb400110j · Cited by 132 · see citing works
Systematic Identification of Cyclic-di-GMP Binding Proteins in Vibrio cholerae Reveals a Novel Class of Cyclic-di-GMP-Binding ATPases Associated with Type II Secretion Systems
Roelofs, K., Jones, C. J., Helman, S. R., Shang, X., Orr, M. W., Goodson, J. R., Galperin, M. Y., Yildiz, F. H., & Lee, V. T. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005232 · Cited by 123 · see citing works
RpoS and the bacterial general stress response
Bouillet, S., Bauer, T., & Gottesman, S. (2024) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00151-22 · Cited by 122 · see citing works
Oxidative stress response in Pseudomonas putida
Kim, J., & Park, W. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5883-4 · Cited by 121 · see citing works
Spaceflight Modifies Escherichia coli Gene Expression in Response to Antibiotic Exposure and Reveals Role of Oxidative Stress Response
Aunins, T. R., Erickson, K. E., Prasad, N., Levy, S., Jones, A., Shrestha, S., Mastracchio, R., Stodieck, L., Klaus, D. M., Zea, L., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00310 · Cited by 110 · see citing works
Evaluation of the metabolic response of Escherichia coli to electrolysed water by 1H NMR spectroscopy
Liu, Q., Wu, J., Lim, Z. Y., Aggarwal, A., Yang, H., & Wang, S. (2017) · LWT · doi:10.1016/j.lwt.2017.01.066 · Cited by 108 · see citing works
Reduce, Induce, Thrive: Bacterial Redox Sensing during Pathogenesis
Reniere, M. L. (2018) · Journal of Bacteriology · doi:10.1128/jb.00128-18 · Cited by 106 · see citing works
Effects of NaCl Concentrations on Growth Patterns, Phenotypes Associated With Virulence, and Energy Metabolism in Escherichia coli BW25113
Li, F., Xiong, X., Yang, Y., Wang, J.-J., Wang, M., Tang, J., Liu, Q., Wang, L., & Gu, B. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.705326 · Cited by 98 · see citing works
Oxidative stress and antioxidant mechanisms of obligate anaerobes involved in biological waste treatment processes: A review
Li, J., Ran, X., Zhou, M., Wang, K., Wang, H., & Wang, Y. (2022) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2022.156454 · Cited by 98 · see citing works
Impact of oxidative stress defense on bacterial survival and morphological change in Campylobacter jejuni under aerobic conditions
Oh, E., McMullen, L. M., & Jeon, B. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00295 · Cited by 97 · see citing works
Regulation of oxidative stress resistance in Campylobacter jejuni, a microaerophilic foodborne pathogen
Kim, J.-C., Oh, E., Kim, J., & Jeon, B. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00751 · Cited by 96 · see citing works
Accelerated evolution of bacterial antibiotic resistance through early emerged stress responses driven by photocatalytic oxidation
Yin, H., Li, G., Chen, X., Wang, W., Wong, P. K., Zhao, H., & An, T. (2020) · Applied Catalysis B: Environmental · doi:10.1016/j.apcatb.2020.118829 · Cited by 92 · see citing works
Corrigendum: Reactive Oxygen Species in Pathogen Clearance: The Killing Mechanisms, the Adaption Response, and the Side Effects
Li, H., Zhou, X., Huang, Y., Liao, B., Cheng, L., & Ren, B. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.685133 · Cited by 90 · see citing works
Microbial oxidative stress response: Novel insights from environmental facultative anaerobic bacteria
Fu, H., Yuan, J., & Gao, H. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.08.012 · Cited by 88 · see citing works
Oxygen: How Do We Stand It?
Fridovich, I. (2012) · Medical Principles and Practice · doi:10.1159/000339212 · Cited by 86 · see citing works
Elimination of antibiotic-resistance bacterium and its associated/dissociative bla and aac(3)-II antibiotic-resistance genes in aqueous system via photoelectrocatalytic process
Jiang, Q., Yin, H., Li, G., Liu, H., An, T., Wong, P. K., & Zhao, H. (2017) · Water Research · doi:10.1016/j.watres.2017.08.050 · Cited by 84 · see citing works
Aminoglycoside uptake, stress, and potentiation in Gram-negative bacteria: new therapies with old molecules
Lang, M., Carvalho, A. F. P., Baharoglu, Z., & Mazel, D. (2023) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00036-22 · Cited by 83 · see citing works
Genome Insights of the Plant-Growth Promoting Bacterium Cronobacter muytjensii JZ38 With Volatile-Mediated Antagonistic Activity Against Phytophthora infestans
Eida, A. A., Bougouffa, S., L’Haridon, F., Alam, I. S., Weisskopf, L., Bajić, V. B., Saad, M. M., & Heribert Hirt, A. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00369 · Cited by 82 · see citing works
DYn-2 Based Identification of Arabidopsis Sulfenomes*
Akter, M. S., Huang, J., Bodra, N., Smet, B. D., Wahni, K., Rombaut, D., Pauwels, J., Gevaert, K., Carroll, K. S., Breusegem, F. V., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.046896 · Cited by 81 · see citing works
Molecular and Structural Characterization of a Novel Escherichia coli Interleukin Receptor Mimic Protein
Moriel, D. G., Heras, B., Paxman, J. J., Lo, A. W. H., Tan, L., Sullivan, M. J., Dando, S. J., Beatson, S. A., Ulett, G. C., & Schembri, M. A. (2016) · mBio · doi:10.1128/mbio.02046-15 · Cited by 80 · see citing works
Food-Associated Stress Primes Foodborne Pathogens for the Gastrointestinal Phase of Infection
Horn, N. L., & Bhunia, A. K. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01962 · Cited by 81 · see citing works
Protection from Oxidative Stress Relies Mainly on Derepression of OxyR-Dependent KatB and Dps in Shewanella oneidensis
Jiang, Y., Dong, Y., Luo, Q., Li, N., Wu, G., & Gao, H. (2013) · Journal of Bacteriology · doi:10.1128/jb.01077-13 · Cited by 78 · see citing works
Acinetobacter baumanniiOxyR Regulates the Transcriptional Response to Hydrogen Peroxide
Juttukonda, L. J., Green, E. R., Lonergan, Z. R., Heffern, M. C., Chang, C. J., & Skaar, E. P. (2019) · Infection and Immunity · doi:10.1128/iai.00413-18 · Cited by 75 · see citing works
Altruism of Shiga toxin-producing Escherichia coli: recent hypothesis versus experimental results
Łoś, J. M., Łoś, M., Węgrzyn, A., & Węgrzyn, G. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00166 · Cited by 71 · see citing works
Employing bacterial mutations for the elucidation of photo-Fenton disinfection: Focus on the intracellular and extracellular inactivation mechanisms induced by UVA and H2O2
Feng, L., Peillex-Delphe, C., Lü, C., Wang, D., Giannakis, S., & Pulgarin, C. O. (2020) · Water Research · doi:10.1016/j.watres.2020.116049 · Cited by 70 · see citing works
Sublethal Photodynamic Treatment Does Not Lead to Development of Resistance
Al-Mutairi, R., Tovmasyan, A. G., Batinic̈‐Haberle, I., & Benov, L. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01699 · Cited by 69 · see citing works
T6SS Mediated Stress Responses for Bacterial Environmental Survival and Host Adaptation
Yu, K., Xue, P., Fu, Y., & Yang, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020478 · Cited by 72 · see citing works
OxyR Is a Convergent Target for Mutations Acquired during Adaptation to Oxidative Stress-Prone Metabolic States
Anand, A., Chen, K., Catoiu, E., Sastry, A. V., Olson, C. A., Sandberg, T. E., Seif, Y., Xu, S., Szubin, R., Yang, L., et al. (2019) · Molecular Biology and Evolution · doi:10.1093/molbev/msz251 · Cited by 68 · see citing works
Genomic data mining of the marine actinobacteria Streptomyces sp. H-KF8 unveils insights into multi-stress related genes and metabolic pathways involved in antimicrobial synthesis
Undabarrena, A., Ugalde, J. A., Seeger, M., & Cámara, B. (2017) · PeerJ · doi:10.7717/peerj.2912 · Cited by 66 · see citing works
Shotgun Proteomic Analysis Unveils Survival and Detoxification Strategies by Caulobacter crescentus during Exposure to Uranium, Chromium, and Cadmium
Yung, M. C., Ma, J., Salemi, M., Phinney, B. S., Bowman, G. R., & Jiao, Y. (2014) · Journal of Proteome Research · doi:10.1021/pr400880s · Cited by 65 · see citing works
Transcriptional Regulation of the CmeABC Multidrug Efflux Pump and the KatA Catalase by CosR in Campylobacter jejuni
Hwang, S., Zhang, Q., Ryu, S., & Jeon, B. (2012) · Journal of Bacteriology · doi:10.1128/jb.01636-12 · Cited by 64 · see citing works
Enhancing E. coli isobutanol tolerance through engineering its global transcription factor cAMP receptor protein (CRP)
Chong, H., Geng, H., Zhang, H., Song, H., Huang, L., & Jiang, R. (2013) · Biotechnology and Bioengineering · doi:10.1002/bit.25134 · Cited by 62 · see citing works
Biological Role of Pigment Production for the Bacterial Phytopathogen Pantoea stewartii subsp. stewartii
Mohammadi, M., Burbank, L. P., & Roper, M. C. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.01574-12 · Cited by 62 · see citing works
Genomic and proteomic evidences unravel the UV-resistome of the poly-extremophile Acinetobacter sp. Ver3
Kurth, D. G., Belfiore, C., Gorriti, M. F., Cortez, N., Farı́as, M. E., & Albarracín, V. H. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00328 · Cited by 58 · see citing works
The antimicrobial action of polyaniline involves production of oxidative stress while functionalisation of polyaniline introduces additional mechanisms
Robertson, J., Gizdavic‐Nikolaidis, M. R., Nieuwoudt, M. K., & Swift, S. (2018) · PeerJ · doi:10.7717/peerj.5135 · Cited by 62 · see citing works
Forged Under the Sun: Life and Art of Extremophiles from Andean Lakes
Albarracín, V. H., Gärtner, W., & Farı́as, M. E. (2015) · Photochemistry and Photobiology · doi:10.1111/php.12555 · Cited by 56 · see citing works
Phenotypic heterogeneity in the bacterial oxidative stress response is driven by cell-cell interactions
Choudhary, D., Lagage, V., Foster, K. R., & Uphoff, S. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112168 · Cited by 57 · see citing works
Expanding the RpoS/σS-Network by RNA Sequencing and Identification of σS-Controlled Small RNAs in Salmonella
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Authors: Chiang, S. M., & Schellhorn, H. E.
Affiliations: McMaster University (CA)
Corresponding author: Schellhorn, Herb E.
ORCID: Schellhorn, Herb E.
Venue: Archives of Biochemistry and Biophysics
Publisher: Elsevier BV
Published: 2012-09
Volume: 525
Issue: 2
Pages: 161-169
ISSN: 0003-9861 (ISSN-L)
DOI: 10.1016/j.abb.2012.02.007
OpenAlex: W2010983045
Cited by: 381
References: 203
Citations by year: 2026: 34 · 2025: 26 · 2024: 34 · 2023: 26 · 2022: 37 · 2021: 28 · 2020: 29 · 2019: 23 · 2018: 25 · 2017: 25 · 2016: 19 · 2015: 26 · 2014: 26 · 2013: 14 · 2012: 9
FWCI: 2.94
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Archives of Biochemistry and Biophysics (publishedVersion)
PubMed (publishedVersion)
Funders: Natural Sciences and Engineering Research Council of Canada
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
Keywords: oxidative stress response, Escherichia coli, OxyR, SoxR, RpoS, reactive oxygen species, hydrogen peroxide resistance, superoxide, transcription factors, positive selection, aerotolerance, gene expression regulation
MeSH terms: Escherichia coli, Genes, Bacterial, Hydrogen Peroxide, Models, Biological, Models, Chemical, Models, Genetic, Protein Conformation, Repressor Proteins, Species Specificity, Superoxide Dismutase, Gene Expression Regulation, Bacterial, Reactive Oxygen Species, Regulon, Oxidative Stress, Bacterial Physiological Phenomena, Escherichia coli Proteins

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Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria

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