Chelation of Cadmium Ions by Phytochelatin Synthase: Role of the Cystein-rich C-Terminal

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  • VESTERGAARD Mun'delanji
    School of Materials Science, Japan Advanced Institute of Science and Technology
  • MATSUMOTO Sachiko
    School of Materials Science, Japan Advanced Institute of Science and Technology
  • NISHIKORI Shingo
    Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University
  • SHIRAKI Kentaro
    Institute of Applied Physics, University of Tsukuba
  • HIRATA Kazumasa
    Department of Environmental Bioengineering Laboratory, Graduate School of Pharmaceutical Sciences, Osaka University
  • TAKAGI Masahiro
    School of Materials Science, Japan Advanced Institute of Science and Technology

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Abstract

The interactions between Cd2+ and the C-terminal region of phytochelatin (PC) synthase using recombinant wild-type and mutant PC synthase were studied. We show that site-directed mutagenesis of Cys residues at C358C359XXXC363XXC366 motif decreases the number of Cd2+ and other heavy metal ions interacting with the enzyme, and that the motif binds the metals discriminatingly. The optimum binding ratio of PC synthase to Cd2+ was also determined. The findings indicate that Cys exists as a free SH residue and that it is involved in the regulation of PC enzyme activity by transferring the metals into closer proximity with the catalytic domain. These results are important in understanding heavy metal detoxification mechanisms in higher plants, a step towards phytoremediated-applications.

Journal

  • Analytical Sciences

    Analytical Sciences 24 (2), 277-281, 2008

    The Japan Society for Analytical Chemistry

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