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Plant and Cell Physiology Advance Access originally published online on January 24, 2007
Plant and Cell Physiology 2007 48(3):434-440; doi:10.1093/pcp/pcm010
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© The Author 2007. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Polyamines as Physiological Regulators of 14-3-3 Interaction with the Plant Plasma Membrane H+-ATPase

Alessandra Garufi, Sabina Visconti, Lorenzo Camoni and Patrizia Aducci*

Department of Biology, University of Rome ‘Tor Vergata’, via della Ricerca Scientifica, I-00133 Rome, Italy

*Corresponding author: E-mail, Aducci{at}uniroma2.it; Fax, +39-06-2023500.


  Abstract

Polyamines are abundant polycationic compounds involved in many plant physiological processes such as cell division, dormancy breaking, plant morphogenesis and response to environmental stresses. In this study, we investigated the possible role of these polycations in modulating the association of 14-3-3 proteins with the H+-ATPase. In vivo experiments demonstrate that, among the different polyamines, spermine brings about 2-fold stimulation of the H+-ATPase activity and this effect is due to an increase in 14-3-3 levels associated with the enzyme. In vivo administration of polyamine synthesis inhibitors causes a small but statistically significant decrease of the H+-ATPase phosphohydrolytic activity, demonstrating a physiological role for the polyamines in regulating the enzyme activity. Spermine stimulates the activity of the H+-ATPase AHA1 expressed in yeast, in the presence of exogenous 14-3-3 proteins, with a calculated S50 of 70 µM. Moreover, spermine enhances the in vitro interaction of 14-3-3 proteins with the H+-ATPase and notably induces 14-3-3 association with the unphosphorylated C-terminal domain of the proton pump. Comparison of spermine with Mg2+, necessary for binding of 14-3-3 proteins to different target proteins, shows that the polyamine effect is stronger than and additive to that of the divalent cation.

Keywords: H+-ATPase - Polyamines - 14-3-3 proteins - Zea mays

Abbreviations: AHA1, Arabidopsis thaliana H+-ATPase isoform 1; bis-ANS, 4,4'-bis(1-anilinonapthalene 8-sulfonate); CHA, cyclohexylamine; DFMO, {alpha}-difluoromethylornithine; GST, glutathione S-transferase; MGBG, methylglyoxal bis-guanylhydrazone; MHA2, Maize H+-ATPase isoform 2; PI, polyamine inhibitor.

(Received December 13, 2006; Accepted January 17, 2007)
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