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The tellurium oxyanion tellurite is harmful for most microorganisms. Since its toxicity occurs chiefly once the toxicant reaches the intracellular compartment, unveiling the toxicant uptake process is crucial for understanding the whole phenomenon of tellurium toxicity. While the PitA phosphate transporter is thought to be one of the main paths responsible for toxicant entry into Escherichia coli, genetic and physiological evidence have identified the ActP acetate carrier as the main tellurite importer in Rhodobacter capsulatus. In this work, new background on the role of these transporters in tellurite uptake by E. coli is presented. It was found that, similar to what occurs in R. capsulatus, ActP is able to mediate toxicant entry to this bacterium. Lower reactive oxygen species levels were observed in E. coli lacking the actP gene. Antioxidant enzyme catalase and fumarase C activity was almost unchanged after short exposure of E. coli ΔactP to sublethal tellurite concentrations, suggesting a low antioxidant response. In this strain, tellurite uptake decreased significantly during the first 5 min of exposure and inductively coupled plasma optical emission spectroscopy assays using an actP-overexpressing strain confirmed that this carrier mediates toxicant uptake. Relative gene expression experiments by qPCR showed that actP expression is enhanced at short times of tellurite exposure, while pitA and pitB genes are induced later. Summarizing, the results show that ActP is involved in tellurite entry to E. coli and that its participation occurs mainly at early stages of toxicant exposure.

The tellurium oxyanion tellurite (TeO32-) is extremely harmful for most organisms. It has been suggested that a potential bacterial tellurite resistance mechanism would consist of an enzymatic, NAD(P)H-dependent, reduction to the less toxic form elemental tellurium (Te0). To date, a number of enzymes such as catalase, type II NADH dehydrogenase and terminal oxidases from the electron transport chain, nitrate reductases, and dihydrolipoamide dehydrogenase (E3), among others, have been shown to display tellurite-reducing activity. This activity is generically referred to as tellurite reductase (TR). Bioinformatic data resting on some of the abovementioned enzymes enabled the identification of common structures involved in tellurite reduction including vicinal catalytic cysteine residues and the FAD/NAD(P)+-binding domain, which is characteristic of some flavoproteins. Along this line, thioredoxin reductase (TrxB), alkyl hydroperoxide reductase (AhpF), glutathione reductase (GorA), mercuric reductase (MerA), NADH: flavorubredoxin reductase (NorW), dihydrolipoamide dehydrogenase, and the putative oxidoreductase YkgC from Escherichia coli or environmental bacteria were purified and assessed for TR activity. All of them displayed in vitro TR activity at the expense of NADH or NADPH oxidation. In general, optimal reducing conditions occurred around pH 9–10 and 37°C. Enzymes exhibiting strong TR activity produced Te-containing nanostructures (TeNS). While GorA and AhpF generated TeNS of 75 nm average diameter, E3 and YkgC produced larger structures (>100 nm). Electron-dense structures were observed in cells over-expressing genes encoding TrxB, GorA, and YkgC.

Mercury salts and tellurite are among the most toxic compounds for microorganisms on Earth. Bacterial mercury resistance is established mainly via mercury reduction by the mer operon system. However, specific mechanisms underlying tellurite resistance are unknown to date. To identify new mechanisms for tellurite detoxification we demonstrate that mercury resistance mechanisms can trigger cross-protection against tellurite to a group of Pseudomonads isolated from the Chilean Antarctic territory. Sequencing of 16S rRNA of four isolated strains resulted in the identification of three Pseudomonads (ATH-5, ATH-41 and ATH-43) and a Psychrobacter (ATH-62) bacteria species. Phylogenetic analysis showed that ATH strains were related to other species previously isolated from cold aquatic and soil environments. Furthermore, the identified merA genes were related to merA sequences belonging to transposons commonly found in isolated bacteria from mercury contaminated sites. Pseudomonas ATH isolates exhibited increased tellurite resistance only in the presence of mercury, especially ATH-43. Determination of the growth curves, minimal inhibitory concentrations and growth inhibition zones showed different tellurite cross-resistance of the ATH strains and suggested a correlation with the presence of a mer operon. On the other hand, reactive oxygen species levels decreased while the thiol content increased when the isolates were grown in the presence of both toxicants. Finally, qPCR determinations of merA, merC and rpoS transcripts from ATH-43 showed a synergic expression pattern upon combined tellurite and mercury treatments. Altogether, the results suggest that mercury could trigger a cell response that confers mercury and tellurite resistance, and that the underlying mechanism participates in protection against oxidative damage.

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Tellurite, the most soluble tellurium oxyanion, is extremely harmful for most microorganisms. Part of this toxicity is due to the generation of reactive oxygen species that in turn cause oxidative stress. However, the way in which tellurite interferes with cellular processes is not well understood to date. Looking for new cellular tellurite targets, we decided to evaluate the functioning of the electron transport chain in tellurite-exposed cells. In this communication we show that the E. coli ndh gene, encoding NDH-II dehydrogenase, is significantly induced in toxicant-exposed cells and that the enzyme displays tellurite-reducing activity that results in increased superoxide levels in vitro.