Novel Antioxidant Role of Alcohol Dehydrogenase E from Escherichia coli

Echave, Pedro; Tamarit, Jordi; Cabiscol, Elisa; Ros, Joaquim

doi:10.1074/jbc.m304351200

Cited by 95 publications

(70 citation statements)

References 50 publications

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“…Manganese metabolism is important during biofilm formation in S. gordonii (Loo et al, 2003) and essential in the pneumococcal colonization of the nasopharynx (Tseng et al, 2002). Iron is an essential cofactor for the function of several enzymes, for example alcohol dehydrogenases, that take part in alternative energetic pathways, and possibly also play a role in the anti-oxidative response (Echave et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Transcriptional analysis of the acid tolerance response in Streptococcus pneumoniae

et al. 2005

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Streptococcus pneumoniae, one of the major causes of morbidity and mortality in humans, faces a range of potentially acidic conditions in the middle and late stages of growth in vitro, in diverse human fluids during the infection process, and in biofilms present in the nasopharynx of carriers. S. pneumoniae was shown to develop a weak acid tolerance response (ATR), where cells previously exposed to sublethal pHs (5?8-6?6) showed an increased survival rate of up to one order of magnitude after challenge at the lethal pH (4?4, survival rate of 10 "4 ).Moreover, the survival after challenge of stationary phase cells at pH 4?4 was three orders of magnitude higher than that of cells taken from the exponential phase, due to the production of lactic acid during growth and increasing acidification of the growth medium until stationary phase. Global expression analysis after short-term (5, 15 and 30 min, the adaptation phase) and long-term (the maintenance phase) acidic shock (pH 6?0) was performed by microarray experiments, and the results were validated by real-time RT-PCR. Out of a total of 126 genes responding to acidification, 59 and 37 were specific to the adaptation phase and maintenance phase, respectively, and 30 were common to both periods. In the adaptation phase, both up-and down-regulation of gene transcripts was observed (38 and 21 genes, respectively), whereas in the maintenance phase most of the affected genes were down-regulated (34 out of 37). Genes involved in protein fate (including those involved in the protection of the protein native structure) and transport (including transporters of manganese and iron) were overrepresented among the genes affected by acidification, 8?7 and 24?6 % of the acid-responsive genes compared to 2?8 % and 9?6 % of the genome complement, respectively. Cross-regulation with the response to oxidative and osmotic stress was observed. Potential regulatory motifs involved in the ATR were identified in the promoter regions of some of the regulated genes.

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Section: Discussionmentioning

confidence: 99%

Transcriptional analysis of the acid tolerance response in Streptococcus pneumoniae

et al. 2005

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“…Peroxide Intracellular Levels-The oxidant-sensitive probe 2Ј,7Ј-dichlorodihydrofluorescein diacetate was used to measure peroxide levels in cells exposed to potassium tellurite (0.5 g/ml), hydrogen peroxide (1 mM), paraquat (50 g/ml), or chromate (1 mM) (24). Cells were grown under aerobic conditions in LB medium amended with the compounds to be tested to an A 600 ϳ 0.3.…”

Section: Methodsmentioning

confidence: 99%

“…Genomic and proteomic studies have shown that YqhD is expressed in E. coli after exposure to stress conditions such as cold shock (21), nutrient starving (22), and oxidative stress generated by the Curvularia peroxidase system (23). YqhD has several features similar to AdhE, an alcohol/aldehyde dehydrogenase involved in fermentative metabolism in E. coli for which an antioxidant function under aerobic conditions has been proposed (24).…”

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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

158

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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“…The intracellular ROS levels in UW136 and MV474 cultures were determined using 29,79-dichlorodihydrofluorescein diacetate (DCFH-DA, Molecular Probes, OR, USA) (Echave et al, 2003). DCFH-DA is cleaved by cellular esterases to 29,79-dichlorodihydrofluorescein (DCFH), and oxidation of DCFH by intracellular ROS gives raise to the fluorescent product 29,79-dichlorofluorescein (DCF).…”

Section: Measurement Of Ros Levelsmentioning

confidence: 99%

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

Remelli

Cereda

Papenbrock

et al. 2010

Biological Chemistry

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The tandem domain rhodanese-homology protein RhdA of Azotobacter vinelandii shows an active-site loop structure that confers structural peculiarity in the environment of its catalytic cysteine residue. The in vivo effects of the lack of RhdA were investigated using an A. vinelandii mutant strain (MV474) in which the rhdA gene was disrupted by deletion. Here, by combining analytical measurements and transcript profiles, we show that deletion of the rhdA gene generates an oxidative stress condition to which A. vinelandii responds by activating defensive mechanisms. In conditions of growth in the presence of the superoxide generator phenazine methosulfate, a stressor-dependent induction of rhdA gene expression was observed, thus highlighting that RhdA is important for A. vinelandii to sustain oxidative stress. The potential of RhdA to buffer general levels of oxidants in A. vinelandii cells via redox reactions involving its cysteine thiol is discussed.

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Novel Antioxidant Role of Alcohol Dehydrogenase E from Escherichia coli

Cited by 95 publications

References 50 publications

Transcriptional analysis of the acid tolerance response in Streptococcus pneumoniae

Transcriptional analysis of the acid tolerance response in Streptococcus pneumoniae

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

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance

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