Enhanced Adsorption and Recovery of Uranyl Ions by NikR Mutant-Displaying Yeast

Kuroda, Kouichi; Ebisutani, Kazuki; Iida, Katsuya; Nishitani, Tadashi; Ueda, Mitsuyoshi

doi:10.3390/biom4020390

Cited by 13 publications

(6 citation statements)

References 17 publications

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“…Later on, Ueda and co-workers showed that the adsorption of UO 2 2+ ions by V72S/H76 D/C95D NikR can be enhanced by displaying the triple mutant on the surface of yeast cells (Figure 4a, right), and the adsorbed UO 2 2+ ions can be recovered by treating the cells with citrate buffer at pH 4.3, which offers a convenient adsorption technique for uranyl enrichment [68]. Inspired by the uranyl coordination, Stellato and Lai recently designed three uranyl-chelating peptides that contain a DG 0-2 DG 0-2 SG 0-2 HG 0-2 H motif [69].…”

Section: Binding To Artificial Metal-binding Sitesmentioning

confidence: 99%

“…Rational design of an artificial uranyl binding site in native and de novo protein scaffolds. (a) Rational design of an artificial UO2 2+ -binding site in NikR by V72S/H76'D/C95D mutations (left)[67], and display of the triple mutant on yeast surface (right)[68]; (b) An X-ray crystal structure of a de novo protein with an artificial UO2 2+ -binding site, and a close-up view of uranyl-binding site, highlighting the coordination and H-bond interactions (PDB code 4FZP, chain B)[10].…”

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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: Binding To Artificial Metal-binding Sitesmentioning

confidence: 99%

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confidence: 99%

Uranyl Binding to Proteins and Structural-Functional Impacts

Lin

2020

Biomolecules

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“…Cell surface engineering technology has also been suggested for the recovery of precious metals from wastewater, for bearing lower costs, and improved selectivity for the target metal compared to conventional methods [ 290 ]. For instance, a mutant protein of E. coli Ni 2+ -dependent transcriptional repressor (NikRm) was shown to selectively bind uranyl ions (UO 2 2+ ) and, thus, significantly increase the recovery of uranium from aqueous solutions when on the cell surface of S. cerevisiae [ 291 ]. In addition, metal-responsive TFs, able to bind and dissociate metal ions, can be repurposed as metal-binding proteins on the cell surface.…”

Section: Genetic Engineering Targets To Improve Microalgal Hm Bioreme...mentioning

confidence: 99%

Is Genetic Engineering a Route to Enhance Microalgae-Mediated Bioremediation of Heavy Metal-Containing Effluents?

Ranjbar

Malcata

2022

Molecules

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Contamination of the biosphere by heavy metals has been rising, due to accelerated anthropogenic activities, and is nowadays, a matter of serious global concern. Removal of such inorganic pollutants from aquatic environments via biological processes has earned great popularity, for its cost-effectiveness and high efficiency, compared to conventional physicochemical methods. Among candidate organisms, microalgae offer several competitive advantages; phycoremediation has even been claimed as the next generation of wastewater treatment technologies. Furthermore, integration of microalgae-mediated wastewater treatment and bioenergy production adds favorably to the economic feasibility of the former process—with energy security coming along with environmental sustainability. However, poor biomass productivity under abiotic stress conditions has hindered the large-scale deployment of microalgae. Recent advances encompassing molecular tools for genome editing, together with the advent of multiomics technologies and computational approaches, have permitted the design of tailor-made microalgal cell factories, which encompass multiple beneficial traits, while circumventing those associated with the bioaccumulation of unfavorable chemicals. Previous studies unfolded several routes through which genetic engineering-mediated improvements appear feasible (encompassing sequestration/uptake capacity and specificity for heavy metals); they can be categorized as metal transportation, chelation, or biotransformation, with regulation of metal- and oxidative stress response, as well as cell surface engineering playing a crucial role therein. This review covers the state-of-the-art metal stress mitigation mechanisms prevalent in microalgae, and discusses putative and tested metabolic engineering approaches, aimed at further improvement of those biological processes. Finally, current research gaps and future prospects arising from use of transgenic microalgae for heavy metal phycoremediation are reviewed.

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“…The adsorption system by yeast cells is effective for simple and concentrated recovery of uranyl ions, as well as adsorption of uranyl ions. 83) To remove or degrade environmental pollutants other than heavy metal ions, engineered yeasts for bioremediation have been constructed. For example, to antagonize endocrine disruptors, which are environmental pollutants that perturb natural endocrine function, the ligand-binding domain of the rat estrogen receptor (ERLBD) has been displayed on S. cerevisiae using the α-agglutinin-based display system.…”

Section: Construction Of Whole-cell Biocatalysts By Cell Surface Engineeringmentioning

confidence: 99%

Establishment of cell surface engineering and its development

Ueda

2016

Bioscience, Biotechnology, and Biochemistry

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Cell surface display of proteins/peptides has been established based on mechanisms of localizing proteins to the cell surface. In contrast to conventional intracellular and extracellular (secretion) expression systems, this method, generally called an arming technology, is particularly effective when using yeasts as a host, because the control of protein folding that is often required for the preparation of proteins can be natural. This technology can be employed for basic and applied research purposes. In this review, I describe various strategies for the construction of engineered yeasts and provide an outline of the diverse applications of this technology to industrial processes such as the production of biofuels and chemicals, as well as bioremediation and health-related processes. Furthermore, this technology is suitable for novel protein engineering and directed evolution through high-throughput screening, because proteins/peptides displayed on the cell surface can be directly analyzed using intact cells without concentration and purification. Functional proteins/peptides with improved or novel functions can be created using this beneficial, powerful, and promising technique.

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Enhanced Adsorption and Recovery of Uranyl Ions by NikR Mutant-Displaying Yeast

Cited by 13 publications

References 17 publications

Uranyl Binding to Proteins and Structural-Functional Impacts

Uranyl Binding to Proteins and Structural-Functional Impacts

Is Genetic Engineering a Route to Enhance Microalgae-Mediated Bioremediation of Heavy Metal-Containing Effluents?

Establishment of cell surface engineering and its development

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