Biological significance of divalent metal ion binding to 14-3-3 proteins in relationship to nitrate reductase inactivation.

@article{Athwal1998BiologicalSO,
  title={Biological significance of divalent metal ion binding to 14-3-3 proteins in relationship to nitrate reductase inactivation.},
  author={G. S. Athwal and J. Huber and S. Huber},
  journal={Plant & cell physiology},
  year={1998},
  volume={39 10},
  pages={
          1065-72
        }
}
  • G. S. Athwal, J. Huber, S. Huber
  • Published 1998
  • Chemistry, Medicine
  • Plant & cell physiology
  • In this report we address two questions regarding the regulation of phosphorylated nitrate reductase (pNR; EC 1.6.6.1) by 14-3-3 proteins. The first concerns the requirement for millimolar concentrations of a divalent cation in order to form the inactive pNR:14-3-3 complex at pH 7.5. The second concerns the reduced requirement for divalent cations at pH 6.5. In answering these questions we highlight a possible general mechanism involved in the regulation of 14-3-3 binding to target proteins. We… CONTINUE READING
    53 Citations

    Topics from this paper

    Divalent cations and polyamines bind to loop 8 of 14-3-3 proteins, modulating their interaction with phosphorylated nitrate reductase.
    • 97
    • PDF
    Function and specificity of 14-3-3 proteins in the regulation of carbohydrate and nitrogen metabolism.
    • 131
    • Highly Influenced
    • PDF
    14-3-3 proteins: eukaryotic regulatory proteins with many functions
    • 98
    Polyamines as physiological regulators of 14-3-3 interaction with the plant plasma membrane H+-ATPase.
    • 58
    • PDF
    The C-terminal tail of Arabidopsis 14-3-3omega functions as an autoinhibitor and may contain a tenth alpha-helix.
    • 35
    Modulation of nitrate reductase: some new insights, an unusual case and a potentially important side reaction.
    • 154
    • Highly Influenced
    • PDF
    Phosphorylated Non-Phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase from Heterotrophic Cells of Wheat Interacts with 14-3-3 Proteins1
    • 44
    • PDF

    References

    SHOWING 1-10 OF 27 REFERENCES
    The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity
    • 1,455