Advances on the toxicity of uranium to different organisms

Gao, Ning; Huang, Zhihui; Liu, Haiqiang; Hou, Jing; Liu, Xinhui

doi:10.1016/j.chemosphere.2019.124548

Cited by 127 publications

(41 citation statements)

References 80 publications

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“…Since UO 2 2+ tends to bind both proteins, especially for Cyt b 5 , the binding of UO 2 2+ to the protein surface may interrupt the interactions of Cyt b 5 -Cyt c complex (Figure 6a). It revealed that the uranyl binding affinity decreases from that of Cyt b 5 (K D = 10 µM) to that of the Cyt b 5 -Cyt c complex (K D = 30 µM), which can be attributed to the dynamic electrostatic interactions between Cyt b 5 and Cyt c such as Glu37-Lys86 that may compete the ligand of Glu37 for uranyl binding [45]. Due to the fact that the protein-protein interactions of Cyt b 5 -Cyt c complex are important in the initiation of apoptosis [46], the disruption of such interactions by UO 2 2+ ions may provide information for understanding uranyl-induced apoptosis [81,82].…”

Section: Disrupting Protein-protein/dna/ligand Interactionsmentioning

confidence: 99%

“…Finally, taking into account of the serious toxic effects of uranyl ion on living systems [3][4][5], it is desired to apply the basic knowledge of uranyl-proteins interactions for seeking approaches for biological remediation of uranyl ions, as well as other heavy metal ions.…”

Section: Fetuin-a 3 Binding Sites~30 Nm-10 µMmentioning

confidence: 99%

“…As widely used in nuclear reactors, uranium, is harmful to living systems due to both the long-lived radioactivity and high toxicity [1,2]. It is especially serious for the toxic effects on human kidneys and lung epithelial cells, such as cell necrosis [3], and osteocytic cells [4], as well as for different organisms, including plants, aquatic invertebrates/vertebrates, bacteria and fungi [5]. The most stable form of uranium under physiological conditions is uranyl ion (UO 2 2+ ), and the high toxicity of uranium might result from the ability of the UO 2 2+ to interact with biomolecules such as nucleotides [6] and proteins [7][8][9], resulting in an alteration or disruption of their native functions.…”

Section: Introductionmentioning

confidence: 99%

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Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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The widespread use of uranium for civilian purposes causes a worldwide concern of its threat to human health due to the long-lived radioactivity of uranium and the high toxicity of uranyl ion (UO 2 2+ ). Although uranyl-protein/DNA interactions have been known for decades, fewer advances are made in understanding their structural-functional impacts. Instead of focusing only on the structural information, this article aims to review the recent advances in understanding the binding of uranyl to proteins in either potential, native, or artificial metal-binding sites, and the structural-functional impacts of uranyl-protein interactions, such as inducing conformational changes and disrupting protein-protein/DNA/ligand interactions. Photo-induced protein/DNA cleavages, as well as other impacts, are also highlighted. These advances shed light on the structure-function relationship of proteins, especially for metalloproteins, as impacted by uranyl-protein interactions. It is desired to seek approaches for biological remediation of uranyl ions, and ultimately make a full use of the double-edged sword of uranium.Proteins, especially for metalloproteins, play vital roles in supporting life, including electron-transfer, O 2 -binding and delivery, and catalysis, etc [11][12][13][14][15][16][17][18]. To date, a plenitude of proteins have been shown to interact with UO 2 2+ , such as proteins in blood (human serum albumin, HSA; transferrin, Tf;hemoglobin, Hb), proteins involved in bone growth (osteopontin, OPN; fetuin-A), and the intracellar proteins (metallothionein, MT; cytochromes b 5 /c; Cyt b 5 /c; calmodulin, CaM), etc [19]. Although the structural features of some uranyl-protein complexes are well-documented [7-9], fewer advances are made in understanding the functional impacts of uranyl-protein interactions, with much less for other actinides-proteins interactions, as reviewed by Creff et al. very recently [20]. Instead of focusing only on the structural information, this review highlights the recent advances in understanding the binding of uranyl to proteins, as illustrated in Scheme 1, in either potential, native or artificial metal-binding sites, or the corresponding structural-functional impacts, such as inducing conformational changes and disrupting protein-protein/DNA/ligand interactions. Future directions for studying uranyl-protein interactions are also prospected.

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Section: Disrupting Protein-protein/dna/ligand Interactionsmentioning

confidence: 99%

Section: Fetuin-a 3 Binding Sites~30 Nm-10 µMmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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“…Natural U is of low radiotoxicity due to its isotopic composition (>99% 238 U) but the uranyl ion (UO 2 2+ ) that is prevalent in oxidizing environments is highly chemotoxic for all living organisms. 4 As predicted by the hard and soft acids and bases principle, 5 UO 2 2+ is a hard acid that reacts preferentially with hard oxygen donors such as phosphate, carboxylate, carbonate and hydroxyl groups, mainly through electrostatic interactions. Therefore, the biological ligands of U can be very diverse, including metabolites, proteins or peptides.…”

Section: Introductionmentioning

confidence: 99%

Development of a metalloproteomic approach to analyse the response of Arabidopsis cells to uranium stress

et al. 2020

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“…The accumulation of U in soil, water and air can pose potential risks to ecosystems, agrosystems, and ultimately human health through food chain contamination, as the radionuclide has both chemical and radiological effects. Natural U is of low radiotoxicity due to its isotopic composition (>99% 238 U) but the uranyl cation (UO 2 2+ ) that is prevalent in oxidizing environments is highly chemotoxic (Gao et al, 2019; Ribera et al, 1996). Since U is not an essential element, its uptake and intracellular trafficking depends on existing metal transporters or channels of broad metal selectivity.…”

Section: Introductionmentioning

confidence: 99%

High-affinity iron and calcium transport pathways are involved in U(VI) uptake in the budding yeast Saccharomyces cerevisiae

Revel

Catty

Ravanel

et al. 2021

Preprint

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Uranium (U) is a naturally-occurring radionuclide toxic for living organisms that can take it up. To date, the mechanisms of U uptake are far from being understood. Here, we used the yeast Saccharomyces cerevisiae as a unicellular eukaryote model to identify U assimilation pathways. Thus, we have identified, for the first time, transport machineries capable of transporting U in a living organism. First, we evidenced a metabolism-dependent U transport in yeast. Then, competition experiments with essential metals allowed us to identify calcium, iron and copper entry pathways as potential routes for U uptake. The analysis of various metal transport mutants revealed that mid1Δ, cch1Δ and ftr1Δ mutants, affected in calcium (Mid1/Cch1 channel) and Fe(III) (Ftr1/Fet3 complex) transport, respectively, exhibited highly reduced U uptake rates and accumulation, demonstrating the implication of these import systems in U uptake. Finally, expression of the Mid1 gene into the mid1Δ mutant restored U uptake levels of the wild type strain, underscoring the central role of the Mid1/Cch1 calcium channel in U absorption process in yeast. Our results also open up the opportunity for rapid screening of U-transporter candidates by functional expression in yeast, before their validation in more complex higher eukaryote model systems.

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Advances on the toxicity of uranium to different organisms

Cited by 127 publications

References 80 publications

Uranyl Binding to Proteins and Structural-Functional Impacts

Uranyl Binding to Proteins and Structural-Functional Impacts

Development of a metalloproteomic approach to analyse the response of Arabidopsis cells to uranium stress

High-affinity iron and calcium transport pathways are involved in U(VI) uptake in the budding yeast Saccharomyces cerevisiae

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