Effects of Fe<sup>3+</sup> and Zn<sup>2+</sup> on the Structural and Thermodynamic Properties of a Soybean ASR Protein

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  • LI Ran-Hui
    Institute of Genetics and Cytology, School of Life Sciences, Northeast Normal University Shenzhen Key Laboratory of Microbiology and Gene Engineering, College of Life Sciences, Shenzhen University
  • LIU Guo-Bao
    Shenzhen Key Laboratory of Microbiology and Gene Engineering, College of Life Sciences, Shenzhen University
  • WANG Hui
    Shenzhen Key Laboratory of Marine Bioresource and Eco-environmental Science, College of Life Sciences, Shenzhen University
  • ZHENG Yi-Zhi
    Shenzhen Key Laboratory of Microbiology and Gene Engineering, College of Life Sciences, Shenzhen University

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  • Effects of Fe³⁺ and Zn²⁺ on the Structural and Thermodynamic Properties of a Soybean ASR Protein

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Abstract

Abscisic acid-, stress-, and ripening-induced (ASR) protein play important roles in protecting plants from abiotic stress. The functions of some ASR proteins are known to be modulated by binding to metal ions. In this study, we demonstrated that the non-tagged full-length soybean (Glycine max) ASR protein (GmASR) can bind Fe3+, Ni2+, Cu2+, and Zn2+. The direct binding properties of GmASR to Fe3+ and Zn2+ were further confirmed by intrinsic fluorescence assays. The GmASR protein was found to have three Fe3+ binding sites but only two Zn2+ binding sites. Natively disordered in aqueous solution, GmASR remained disordered in the presence of Fe3+, but was found to aggregate in the presence of Zn2+. The aggregated GmASR protein was partially resolubilized after Zn2+ was chelated by EDTA. GmASR exhibited Fe3+-binding-dependent antioxidant activity in vitro. We speculate that GmASR thus protects against oxidation damage by buffering metal ions, thus alleviating metal toxicity in plant cells under stressed conditions.

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