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Divalent cation binding to wheat germ calmodulin.

M Yoshida, O Minowa, K Yagi

    Journal of Biochemistry
    |December 1, 1983
    PubMed
    Summary
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    Wheat germ calmodulin binds calcium ions with varying affinities. The third calcium binding site is near Cysteine 27, and the first manganese ion binds to the N-terminal domain.

    Area of Science:

    • Biochemistry
    • Molecular Biology

    Background:

    • Calmodulin is a crucial calcium-binding protein involved in cellular signaling.
    • Understanding metal ion binding to calmodulin provides insights into its regulatory mechanisms.

    Purpose of the Study:

    • To quantify calcium ion binding to wheat germ calmodulin.
    • To investigate the location of calcium and manganese binding sites on wheat germ calmodulin.

    Main Methods:

    • Flow-dialysis method to measure Ca2+ binding constants.
    • Quantitative analysis of DTNB reaction with Cys 27.
    • Electron Spin Resonance (ESR) spectroscopy of spin-labeled calmodulin with Mn2+ and Ca2+.

    Main Results:

    • Four macroscopic binding constants for Ca2+ were determined (0.20, 0.25, 0.025, 0.0024 microM-1).

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  • The third Ca2+ binding site is located near Cys 27.
  • ESR data indicated the first Mn2+ binds to the N-terminal domain, approximately 0.8 nm from the spin label at Cys 27.

    • Conclusions:

    • Wheat germ calmodulin exhibits distinct Ca2+ binding affinities.
    • Cys 27 is in proximity to the third Ca2+ binding site.
    • Mn2+ binding to the N-terminal domain influences calmodulin structure.