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

被引:271
|
作者
Chiang, Sarah M. [1 ]
Schellhorn, Herb E. [1 ]
机构
[1] McMaster Univ, Dept Biol, Hamilton, ON L8S 4K1, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
Catalase; Bacteria; Regulation; Stress; Stationary phase; Oxidation; Free radical; Sigma factor; FERRIC UPTAKE REGULATION; MULTIPLE-ANTIBIOTIC-RESISTANCE; ALKYL HYDROPEROXIDE REDUCTASE; NITRIC-OXIDE REDUCTION; DNA-BINDING SITES; SIGMA-FACTOR RPOS; KATG-DPSA OPERON; HYDROGEN-PEROXIDE; SUPEROXIDE-DISMUTASE; MYCOBACTERIUM-TUBERCULOSIS;
D O I
10.1016/j.abb.2012.02.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 H2O2 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. (c) 2012 Elsevier Inc. All rights reserved.
引用
收藏
页码:161 / 169
页数:9
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