Journal Article

Biological Significance of Divalent Metal Ion Binding to 14-3-3 Proteins In Relationship to Nitrate Reductase Inactivation<sup>1</sup>

Gurdeep S. Athwal, Joan L. Huber and Steven C. Huber

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 39, issue 10, pages 1065-1072
Published in print October 1998 | ISSN: 0032-0781
Published online October 1998 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029303
Biological Significance of Divalent Metal Ion Binding to 14-3-3 Proteins In Relationship to Nitrate Reductase Inactivation1

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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 show that divalent cations (e.g. Ca2+, Mg2+ and Mn2+) bind directly to 14-3-3s, and as a result cause a conformational change, manifested as an increase in surface hydrophobicity. A similar change is also obtained by decreasing the pH from pH 7.5 to pH 6.5, in the absence of divalent cations, and we propose that protonation of amino acid residues brings about a similar effect to metal ion binding. A possible regulatory mechanism, where the 14-3-3 protein has to be “primed” prior to binding a target protein, is discussed.

Keywords: 14-3-3 protein; Conformational change; Fluorescence; Metal binding site; Nitrate reductase; Protonation

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Subjects: Plant Sciences and Forestry ; Biochemistry ; Molecular and Cell Biology

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