Glutathione in Escherichia coli is dispensable for resistance to H2O2 and gamma radiation

Greenberg, Jean T.; Demple, Bruce

doi:10.1128/jb.168.2.1026-1029.1986

Cited by 141 publications

(102 citation statements)

References 23 publications

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“…S1) GSH is a predominant low molecular weight thiol in E. coli, as in the case of many other organisms, and it has been proposed to protect cells from oxidative damages such as those caused by H 2 O 2 and ionizing radiations (28). However, it has been reported that a ⌬gshA mutation does not cause increased sensitivities to H 2 O 2 or cumene hydroperoxide (29). In addition, we, ourselves, observed here that there was no detectable change in the levels of resistance to H 2 O 2 between the wild-type cells and the ⌬gshA mutant whether or not YdeD is overproduced (Fig.…”

Section: Discussionmentioning

confidence: 99%

The l-Cysteine/l-Cystine Shuttle System Provides Reducing Equivalents to the Periplasm in Escherichia coli

Ohtsu¹,

Wiriyathanawudhiwong²,

Morigasaki

et al. 2010

Journal of Biological Chemistry

111

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Intracellular thiols like L-cysteine and glutathione play a critical role in the regulation of cellular processes. Escherichia coli has multiple L-cysteine transporters, which export L-cysteine from the cytoplasm into the periplasm. However, the role of L-cysteine in the periplasm remains unknown. Here we show that an L-cysteine transporter, YdeD, is required for the tolerance of E. coli cells to hydrogen peroxide. We also present evidence that L-cystine, a product from the oxidation of L-cysteine by hydrogen peroxide, is imported back into the cytoplasm in a manner dependent on FliY, the periplasmic L-cystine-binding protein. Remarkably, this protein, which is involved in the recycling of the oxidized L-cysteine, is also found to be important for the hydrogen peroxide resistance of this organism. Furthermore, our analysis of the transcription of relevant genes revealed that the transcription of genes encoding FliY and YdeD is highly induced by hydrogen peroxide rather than by L-cysteine. These findings led us to propose that the inducible L-cysteine/Lcystine shuttle system plays an important role in oxidative stress tolerance through providing a reducing equivalent to the periplasm in E. coli.

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Section: Discussionmentioning

confidence: 99%

The l-Cysteine/l-Cystine Shuttle System Provides Reducing Equivalents to the Periplasm in Escherichia coli

Ohtsu¹,

Wiriyathanawudhiwong²,

Morigasaki

et al. 2010

Journal of Biological Chemistry

111

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“…5). In aerobically growing E. coli cells, there is about 0.39 mol of L-cysteine/10 12 cells, which is equivalent to an intracellular concentration of 0.2 mM L-cysteine (41). This concentration of L-cysteine may be sufficient to remove the dinitrosyl iron complexes when the cells are exposed to a single dose of nitric oxide (at a final concentration of about 5 M) used in this study (Fig.…”

Section: Discussionmentioning

confidence: 99%

l-Cysteine-mediated Destabilization of Dinitrosyl Iron Complexes in Proteins

Rogers

Ding

2001

Journal of Biological Chemistry

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Nitric oxide is a signaling molecule in intercellular communication as well as a powerful weapon used by macrophages to kill tumor cells and pathogenic bacteria. Here, we show that when Escherichia coli cells are exposed to nitric oxide, its ferredoxin [2Fe-2S] cluster is nitrosylated, forming the dinitrosyl iron complex with a characteristic EPR signal at g av ‫؍‬ 2.04. Such formed ferredoxin dinitrosyl iron complex is efficiently repaired in E. coli cells even in the absence of new protein synthesis. However, the repair activity is completely inactivated once E. coli cells are disrupted, indicating that repairing the ferredoxin dinitrosyl iron complex requires cellular reducing equivalents. In search of such cellular factors, we find that L-cysteine can effectively eliminate the EPR signal of the ferredoxin dinitrosyl iron complex and release the ferrous iron from the complex. In contrast, N-acetyl-L-cysteine and reduced glutathione are much less effective. L-Cysteine seems to have a general function, since it can also remove the otherwise stable dinitrosyl iron complexes from proteins in the cell extracts prepared from the E. coli cells treated with nitric oxide. We propose that L-cysteine is responsible for removing the dinitrosyl iron complexes from the nitric oxide-modified proteins into which a new iron-sulfur cluster will be reassembled.

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“…We further tested this hypothesis by making our uvrB5 E. coli strains gshA20:: Tn10kan. Bacteria with this mutation have no detectable glutathione activity (Greenberg and Demple, 1986). As shown in Figs.…”

Section: The Effect Of Metabolic Activation On Edb Mutagenicitymentioning

confidence: 96%

An analysis of the mutagenicity of 1,2-dibromoethane to Escherichia coli: Influence of DNA repair activities and metabolic pathways

Foster

Wilkinson

Miller

et al. 1988

Mutation Research/DNA Repair Reports

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SummaryThe mutagenicity of 1,2-dibromoethane (EDB) to Escherichia coli was reduced by the UV lightinduced excision repair system but unaffected by the loss of a major apurinic/apyrimidinic site repair function. At high doses, 70-90% of the EDB-induced mutations were independent of SOS-mutagenic processing and approximately 50% were independent of glutathione conjugation. The SOSindependent mutations induced by EDB were unaffected by the enzymes that repair alkylationinduced DNA lesions. EDB-induced base substitutions were dominated by GC to AT and AT to GC transitions. These results suggest that EDB-induced premutagenic lesions have some, but not all, of the characteristics of simple alkyl lesions. KeywordsDibromoethane; EDB; Escherichia coil; Miscoding lesions; DNA repair 1,2-Dibromoethane (EDB or DBE; has been used as an antiknock additive in leaded gasoline, an industrial solvent, a pesticide, and a food disinfectant (NIOSH, 1977). It is one of a class of potentially hazardous compounds, the haloalkanes, that has become widely distributed in the environment . EDB is highly toxic, causing liver and kidney necrosis and reproductive abnormalities (reviews Shih and Hill, 1981;Rannug, 1980;Ter Haar, 1980). It has been repeatedly shown to be carcinogenic to rodents, resulting in tumors in a number of organs, including the forestomach, liver, spleen and thyroid (NCI, 1978). Thus environmental exposure to EDB is a potential health hazard.The mutagenicity of EDB has been demonstrated in a number of genetic systems, including bacteria, yeast and other fungi, plants, insects, mammals and human cells (reviews, Fabricant and Chalmers, 1980;Rannug, 1980). Although EDB is a direct-acting mutagen in the Salmonella/microsome assay (McCann et al., 1975a), its mutagenicity has been shown to be further enhanced by metabolic activation (Rannug, 1980). Metabolic activation of EDB to its ultimate mutagenic and carcinogenic form has been hypothesized to occur by two different (Rannug, 1980; Anders and Livesey, 1980). One, mediated by the mixed-function oxygenases of liver microsomes, would yield bromoacetaldehyde and 2-bromoethanol as potential DNA-damaging agents (Hill et al., 1978;Banerjee et al., 1979). The other pathway, conjugation with glutathione mediated by enzymes present in liver cytosol, would yield as reactive products a half-sulfur-mustard or an episulfonium ion (Rannug, 1980;van Bladeren et al., 1980). The binding of EDB to DNA in vitro has been shown to be dependent on glutathione conjugation, and an S- [2-(N 7 -guanyl)ethyl]glutathione adduct has been identified (Ozawa and Guengerich, 1983;Inskeep and Guengerich, 1984). However, bromoacetaldehyde is a metabolite of EDB (Hill et al., 1978) and can bind to DNA without enzymatic activation (Banerjee et al., 1979). Both 2-bromoethanol and chloroacetaldehyde are bacterial mutagens (McCann et al., 1975b;Rannug et al., 1976;Rosenkranz, 1977), but bromoacetaldehyde is not, possibly due to its extreme toxicity (Rosenkranz, 1977). Thus, the identity of the genotoxic metabol...

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Glutathione in Escherichia coli is dispensable for resistance to H2O2 and gamma radiation

Cited by 141 publications

References 23 publications

The l-Cysteine/l-Cystine Shuttle System Provides Reducing Equivalents to the Periplasm in Escherichia coli

The l-Cysteine/l-Cystine Shuttle System Provides Reducing Equivalents to the Periplasm in Escherichia coli

l-Cysteine-mediated Destabilization of Dinitrosyl Iron Complexes in Proteins

An analysis of the mutagenicity of 1,2-dibromoethane to Escherichia coli: Influence of DNA repair activities and metabolic pathways

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