Tellurite-mediated thiol oxidation in Escherichia coli

Turner, Raymond J.; Weiner, Joël H.; Taylor, Diane E.

doi:10.1099/00221287-145-9-2549

Cited by 127 publications

(148 citation statements)

References 52 publications

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“…As was observed by Turner et al (1999Turner et al ( , 2001) tellurite causes thiol oxidation, compromising seriously the redox balance of the cell. Moreover, superoxide generated as byproduct of tellurite reduction (Pérez et al, 2007) (Massey, 1994;Messner & Imlay, 1999, 2002.…”

Section: Discussionmentioning

confidence: 99%

Tellurite-mediated disabling of [4Fe–4S] clusters of Escherichia coli dehydratases

et al. 2009

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The tellurium oxyanion tellurite is toxic for most organisms and it seems to alter a number of intracellular targets. In this work the toxic effects of tellurite upon Escherichia coli [4Fe-4S] cluster-containing dehydratases was studied. Reactive oxygen species (ROS)-sensitive fumarase A (FumA) and aconitase B (AcnB) as well as ROS-resistant fumarase C (FumC) and aconitase A (AcnA) were assayed in cell-free extracts from tellurite-exposed cells in both the presence and absence of oxygen. While over 90 % of FumA and AcnB activities were lost in the presence of oxygen, no enzyme inactivation was observed in anaerobiosis. This result was not dependent upon protein biosynthesis, as determined using translation-arrested cells. Enzyme activity of purified FumA and AcnB was inhibited when exposed to an in vitro superoxide-generating, telluritereducing system (ITRS). No inhibitory effect was observed when tellurite was omitted from the ITRS. In vivo and in vitro reconstitution experiments with tellurite-damaged FumA and AcnB suggested that tellurite effects involve [Fe-S] cluster disabling. In fact, after exposing FumA to ITRS, released ferrous ion from the enzyme was demonstrated by spectroscopic analysis using the specific Fe 2+ chelator 2,29-bipyridyl. Subsequent spectroscopic paramagnetic resonance analysis of FumA exposed to ITRS showed the characteristic signal of an oxidatively inactivated [3Fe-4S] + cluster. These results suggest that tellurite inactivates enzymes of this kind via a superoxide-dependent disabling of their [4Fe-4S] catalytic clusters.

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Section: Discussionmentioning

confidence: 99%

Tellurite-mediated disabling of [4Fe–4S] clusters of Escherichia coli dehydratases

et al. 2009

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“…Among the highly induced genes implicated in oxidative stress resistance are the catalase gene katE (DR1998), terB (DR2220), terZ (DR2224), msrA (DR1849), dps2 (DRB0092) (602), and five genes of the Nudix hydrolase family, including the MutT ortholog (368). The tellurium resistance proteins TerB and TerZ maintain the intracellular reducing environment in E. coli, possibly by directly reversing disulfide bonds (626), and confer resistance to various damaging agents, such as heavy metal ions, MMS, MMC, and UV radiation (31). MsrA is a methionine sulfoxide reductase, while Dps2 is a DNA binding protein, which presumably protects DNA from oxidative damage (11,390,668).…”

Section: Induction Of Gene Expression and Protein Synthesis In Responmentioning

confidence: 99%

Oxidative Stress Resistance inDeinococcus radiodurans

Slade

Radman

2011

Microbiol Mol Biol Rev

648

639

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SUMMARY Deinococcus radiodurans is a robust bacterium best known for its capacity to repair massive DNA damage efficiently and accurately. It is extremely resistant to many DNA-damaging agents, including ionizing radiation and UV radiation (100 to 295 nm), desiccation, and mitomycin C, which induce oxidative damage not only to DNA but also to all cellular macromolecules via the production of reactive oxygen species. The extreme resilience of D. radiodurans to oxidative stress is imparted synergistically by an efficient protection of proteins against oxidative stress and an efficient DNA repair mechanism, enhanced by functional redundancies in both systems. D. radiodurans assets for the prevention of and recovery from oxidative stress are extensively reviewed here. Radiation- and desiccation-resistant bacteria such as D. radiodurans have substantially lower protein oxidation levels than do sensitive bacteria but have similar yields of DNA double-strand breaks. These findings challenge the concept of DNA as the primary target of radiation toxicity while advancing protein damage, and the protection of proteins against oxidative damage, as a new paradigm of radiation toxicity and survival. The protection of DNA repair and other proteins against oxidative damage is imparted by enzymatic and nonenzymatic antioxidant defense systems dominated by divalent manganese complexes. Given that oxidative stress caused by the accumulation of reactive oxygen species is associated with aging and cancer, a comprehensive outlook on D. radiodurans strategies of combating oxidative stress may open new avenues for antiaging and anticancer treatments. The study of the antioxidation protection in D. radiodurans is therefore of considerable potential interest for medicine and public health.

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“…These results suggested that YqhD may play an antioxidant role by protecting E. coli from the oxidative damage caused specifically by ROS. This YqhD function would be of particular importance when cells encounter compounds that generate superoxide (tellurite) or hydroxyl radicals (chromate) (4, 5) since these toxics also affect cytoplasmic GSH levels (9,29,30). In this context, the hypersensitive phenotype to K 2 TeO 3 and K 2 Cr 2 O 7 observed in E. coli ⌬yqhD could be explained by a dual effect caused by ROS, namely the known direct damage on proteins, DNA, and membrane lipids and, indirectly, the inherent toxicity of peroxides and reactive aldehydes generated by membrane lipid peroxidation, which could not be scavenged in the absence of GSH.…”

Section: Figure 3 Oxidized Proteins In E Coli a Sds-page Showing mentioning

confidence: 99%

Escherichia coli YqhD Exhibits Aldehyde Reductase Activity and Protects from the Harmful Effect of Lipid Peroxidation-derived Aldehydes

Pérez¹,

Arenas²,

Pradenas³

et al. 2008

Journal of Biological Chemistry

154

135

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Evidence that Escherichia coli YqhD is involved in bacterial response to compounds that generate membrane lipid peroxidation is presented. Overexpression of yqhD results in increased resistance to the reactive oxygen species-generating compounds hydrogen peroxide, paraquat, chromate, and potassium tellurite. Increased tolerance was also observed for the lipid peroxidation-derived aldehydes butanaldehyde, propanaldehyde, acrolein, and malondialdehyde and the membrane-peroxidizing compound tert-butylhydroperoxide. Expression of yqhD was also associated with changes in the concentration of intracellular peroxides and cytoplasmic protein carbonyl content and with a reduction in intracellular acrolein levels. When compared with the wild type strain, an yqhD mutant exhibited a sensitive phenotype to all these compounds and also augmented levels of thiobarbituric acid-reactive substances, which may indicate an increased level of lipid peroxidation. Purified YqhD catalyzes the in vitro reduction of acetaldehyde, malondialdehyde, propanaldehyde, butanaldehyde, and acrolein in a NADPH-dependent reaction. Finally, yqhD transcription was induced in cells that had been exposed to conditions favoring lipid peroxidation. Taken together these results indicate that this enzyme may have a physiological function by protecting the cell against the toxic effect of aldehydes derived from lipid oxidation. We speculate that in Escherichia coli YqhD is part of a glutathione-independent, NADPH-dependent response mechanism to lipid peroxidation.

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Tellurite-mediated thiol oxidation in Escherichia coli

Cited by 127 publications

References 52 publications

Tellurite-mediated disabling of [4Fe–4S] clusters of Escherichia coli dehydratases

Tellurite-mediated disabling of [4Fe–4S] clusters of Escherichia coli dehydratases

Oxidative Stress Resistance inDeinococcus radiodurans

Escherichia coli YqhD Exhibits Aldehyde Reductase Activity and Protects from the Harmful Effect of Lipid Peroxidation-derived Aldehydes

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