The Cu(II)-reductase NADH dehydrogenase-2 of Escherichia coli improves the bacterial growth in extreme copper concentrations and increases the resistance to the damage caused by copper and hydroperoxide

Rodrı́guez-Montelongo, Luisa; Volentini, Sabrina Inès; Farı́as, Ricardo N.; Massa, Eddy M.; Rapisarda, Viviana Andrea

doi:10.1016/j.abb.2006.04.019

Cited by 50 publications

(34 citation statements)

References 26 publications

(37 reference statements)

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“…In agreement with the results obtained with NDH-2 (Rodríguez- Montelongo et al 2006), quinone absence avoided the cellular growth in medium containing either high or low copper concentrations. Thus, these respiratory chain components allow the resistance to high metal concentration maybe by their involvement in Cu(II)-reductase activity.…”

Section: Discussionsupporting

confidence: 91%

“…Considering that Cu(II)-reduction is a central mechanism related to copper homeostasis (Solioz and Stoyanov 2003;Rensing and Grass 2003;Rodríguez-Montelongo et al 2006), the in vivo studies about this topics gain importance. Here, we were able to measure the Cu(II)-reductase activity in living E. coli cells, using the sublethal copper concentration 0.2 mM, which is in agreement with the range applied in studies with whole cells of Lactococcus lactis (Rezaïki et al 2008).…”

Section: Discussionmentioning

confidence: 99%

“…Growth of quinone mutants in media with excess or deficiency of copper NDH-2 mutants did not grow in media containing high or low copper concentration (Rodríguez-Montelongo et al 2006). For these previous experiments, we have used citrate as a suitable chelator to modulate the free metal concentration available for the cells, since it has a relative low affinity for aqueous Cu(II) ions [association constant *10 5.9 M] (Dawson et al 1986).…”

Section: Fe(iii) Reduction By Bacterial Suspensionsmentioning

confidence: 98%

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Cu(II)-reduction by Escherichia coli cells is dependent on respiratory chain components

Volentini

Farı́as

Rodrı́guez-Montelongo

et al. 2011

Biometals

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Copper is both an essential nutrient and a toxic element able to catalyze free radicals formation which damage lipids and proteins. Although the available copper redox species in aerobic environment is Cu(II), proteins that participate in metal homeostasis use Cu(I). With isolated Escherichia coli membranes, we have previously shown that electron flow through the respiratory chain promotes cupric ions reduction by NADH dehydrogenase-2 and quinones. Here, we determined Cu(II)-reductase activity by whole cells using strains deficient in these respiratory chain components. Measurements were done by the appearance of Cu(I) in the supernatants of cells exposed to sub-lethal Cu(II) concentrations. In the absence of quinones, the Cu(II)-reduction rate decreased ~70% in respect to the wild-type strain, while this diminution was about 85% in a strain lacking both NDH-2 and quinones. The decrease was ~10% in the absence of only NDH-2. In addition, we observed that quinone deficient strains failed to grow in media containing either excess or deficiency of copper, as we have described for NDH-2 deficient mutants. Thus, the Cu(II)-reduction by E. coli intact cells is mainly due to quinones and to a lesser extent to NDH-2, in a quinone-independent way. To our knowledge, this is the first in vivo demonstration of the involvement of E. coli respiratory components in the Cu(II)-reductase activity which contributes to the metal homeostasis.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Section: Fe(iii) Reduction By Bacterial Suspensionsmentioning

confidence: 98%

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Cu(II)-reduction by Escherichia coli cells is dependent on respiratory chain components

Volentini

Farı́as

Rodrı́guez-Montelongo

et al. 2011

Biometals

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“…In contrast to NDH-1, NDH-2 (encoded by the ndh gene) catalyses the reoxidation of NADH exclusively and transfers electrons to ubiquinone-1 (Calhounand Gennis, 1993; Gyan et al, 2006). In the cell, NDH-2 links the major catabolic and energy-producing pathways (Jaworowski et al, 1981) that contribute in the bacterial oxidative and stress protection (Rapisarda et al, 2002;Rodriguez-Montelongo et al, 2006). In this study, we found that the physiological role of UdhA was correlated with the expression level of NDH-2.…”

Section: Effect On Ndh-2 Expressionmentioning

confidence: 99%

Physiologic roles of soluble pyridine nucleotide transhydrogenase inEscherichia coli as determined by homologous recombination

et al. 2008

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The soluble transhydrogenase is an energy-independent flavoprotein and important in cofactor regenerating system. In order to understand its physiologic roles, the recombinant strain with the deletion of soluble transhydrogenase gene (ΔudhA) in Escherichia coli was constructed using homologous recombination. Then the different genetic backgrounds containing either icd NADP or icd NAD , which encodes NADP-dependent isocitrate dehydrogenase (IDH) or engineered NAD-dependent IDH, were transduced into ΔudhA, creating two strains (icd NADP /ΔudhA, icd NAD /ΔudhA). During growth on acetate, icd NADP /ΔudhA grew poorly and its growth rate was remarkably reduced by 75% as compared with the wild type. However, icd NAD /ΔudhA showed significantly better growth than icd NADP /ΔudhA. Its growth rate was about 3.7 fold of icd NADP /ΔudhA, which was equivalent to the wild type. These results indicated that UdhA is an essential NADH resource for acetate-grown E. coli and is a dominant factor for bacteria to adapt to the stress environment. Furthermore, when UdhA was absence, icd NAD /ΔudhA displayed about 1.5 fold increase in the IDH activity after switching the carbon source from glucose to acetate. And RT-PCR showed that the expression of NADH dehydrogenase II (NDH-2) in icd NAD /ΔudhA was remarkably up-regulated by about 2.8 fold as compared with icd NADP /ΔudhA. The increase of IDH activity and NDH-2 expression can be explained by the reducing excess NADPH production and restoring higher levels of NADH generation in cells.

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“…In MTϩP medium-grown cells, membrane NDH-2 and succinate dehydrogenase activities (18,21,24) decreased through stationary phase in the mutant strain, whereas they remained high in the wild-type strain (Table 2). In addition, catalase on May 12, 2018 by guest http://jb.asm.org/ activity (7,25) increased in the wild-type strain only during stationary phase (Table 2).…”

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confidence: 99%

Phosphate-Enhanced Stationary-Phase Fitness of Escherichia coli Is Related to Inorganic Polyphosphate Level

et al. 2009

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We found that Escherichia coli grown in media with >37 mM phosphate maintained a high polyphosphate level in late stationary phase, which could account for changes in gene expression and enzyme activities that enhance stationary-phase fitness.Polyphosphate (poly-P) is a long-chain polymer composed of many orthophosphates linked together by high-energy ATPlike bonds. Studied mainly in prokaryotes, poly-P plays an important role as an energy source, as a regulator of gene expression, as a store of inorganic phosphate, and as a chelator of heavy metals (8, 10). The main enzymes associated with poly-P metabolism in bacteria are the polyphosphate kinase (PPK, encoded by ppk) and the exopolyphosphatase (PPX, encoded by ppx) (1, 2). The ppk ppx double mutant exhibits greatly reduced synthesis of poly-P, is deficient in stationaryphase functions, and lacks resistance to different stresses (6,17).Previously, we found that expression of several respiratory (ndh, sdhC, ubiC, nuoAB, and cydA) and defense (katG and ahpC) genes was maintained in late stationary phase when the medium's phosphate concentration was above 37 mM (24, 25). Furthermore, Escherichia coli cells grown in medium containing this critical phosphate concentration had high viability, low oxidative damage, and elevated resistance to external H 2 O 2 stress in late stationary phase (25).We examined the relationship between the medium's phosphate concentration and intracellular poly-P levels in the wildtype and ppk ppx mutant strains to see if the previously observed effects on gene expression, enzyme activity, and tolerance to H 2 O 2 were correlated with elevated poly-P levels.Measurements of poly-P level in whole cells. Intracellular poly-P was measured in cell suspensions by using a DAPI (4Ј,6-diamidino-2-phenylindole)-based fluorescence approach (3). Cells were washed and resuspended in buffer T (100 mM Tris HCl [pH 7.5]). DAPI (Sigma) was added to 10 M in cuvettes containing cell suspensions in buffer T at an optical density at 560 nm of 0.02. After 5 min of agitation at 37°C, the DAPI fluorescence spectra (excitation, 415 nm; emission, 445 to 650 nm) were recorded using an ISS PCI spectrofluorometer (Champaign, IL). The fluorescence (in arbitrary units) of the DAPI-poly-P complex at 550 nm was used as a measure of intracellular poly-P because fluorescence emissions from free DAPI and from DAPI-DNA are minimal at this wavelength (3).We first compared various conditions for preparing the cell samples, using exponential-phase cells grown aerobically in LB medium at 37°C (Fig.

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The Cu(II)-reductase NADH dehydrogenase-2 of Escherichia coli improves the bacterial growth in extreme copper concentrations and increases the resistance to the damage caused by copper and hydroperoxide

Cited by 50 publications

References 26 publications

Cu(II)-reduction by Escherichia coli cells is dependent on respiratory chain components

Cu(II)-reduction by Escherichia coli cells is dependent on respiratory chain components

Physiologic roles of soluble pyridine nucleotide transhydrogenase inEscherichia coli as determined by homologous recombination

Phosphate-Enhanced Stationary-Phase Fitness of Escherichia coli Is Related to Inorganic Polyphosphate Level

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