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Biomolecules 2014, 4(2), 390-401;

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

Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
Author to whom correspondence should be addressed.
Received: 4 February 2014 / Revised: 12 March 2014 / Accepted: 14 March 2014 / Published: 11 April 2014
(This article belongs to the Special Issue Metal Binding Proteins)
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Uranium is one of the most important metal resources, and the technology for the recovery of uranyl ions (UO22+) from aqueous solutions is required to ensure a semi-permanent supply of uranium. The NikR protein is a Ni2+-dependent transcriptional repressor of the nickel-ion uptake system in Escherichia coli, but its mutant protein (NikRm) is able to selectively bind uranyl ions in the interface of the two monomers. In this study, NikRm protein with ability to adsorb uranyl ions was displayed on the cell surface of Saccharomyces cerevisiae. To perform the binding of metal ions in the interface of the two monomers, two metal-binding domains (MBDs) of NikRm were tandemly fused via linker peptides and displayed on the yeast cell surface by fusion with the cell wall-anchoring domain of yeast α-agglutinin. The NikRm-MBD-displaying yeast cells with particular linker lengths showed the enhanced adsorption of uranyl ions in comparison to the control strain. By treating cells with citrate buffer (pH 4.3), the uranyl ions adsorbed on the cell surface were recovered. Our results indicate that the adsorption system by yeast cells displaying tandemly fused MBDs of NikRm is effective for simple and concentrated recovery of uranyl ions, as well as adsorption of uranyl ions. View Full-Text
Keywords: cell surface engineering; arming yeast; bioadsorption; uranyl ions; NikR cell surface engineering; arming yeast; bioadsorption; uranyl ions; NikR

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Kuroda, K.; Ebisutani, K.; Iida, K.; Nishitani, T.; Ueda, M. Enhanced Adsorption and Recovery of Uranyl Ions by NikR Mutant-Displaying Yeast. Biomolecules 2014, 4, 390-401.

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