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• W2079807699 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." @default.
• W2079807699 created "2016-06-24" @default.
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• W2079807699 date "2013-03-23" @default.
• W2079807699 modified "2023-10-16" @default.
• W2079807699 title "Effects of Fe³⁺and Zn²⁺on the Structural and Thermodynamic Properties of a Soybean ASR Protein" @default.
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• W2079807699 doi "https://doi.org/10.1271/bbb.120666" @default.
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