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Characterization of Spermidine Binding to Solubilized Plasma Membrane Proteins from Zucchini Hypocotyls1

Annalisa Tassoni, Fabiana Antognoni, Maria Luisa Battistini, Olivier Sanvido, and Nello Bagni*

Dipartimento di Biologia Evoluzionistica Sperimentale, Università di Bologna, Via Irnerio 42, 40126 Bologna, Italy

In this work [14C]spermidine binding to total proteins solubilized from plasma membrane purified from zucchini (Cucurbita pepo L.) hypocotyls was investigated. Proteins were solubilized using octyl glucoside as a detergent. Specific polyamine binding was thermolabile, reversible, pH dependent with an optimum at pH 8.0, and had a Kd value of 5 µM, as determined by glass-fiber-filter assays. Sephadex G-25 M gel-filtration assays confirmed the presence of a spermidine-protein(s) complex with a specific binding activity. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis and native polyacrylamide gel electrophoresis of collected fractions having the highest specific spermidine-binding activity, several protein bands (113, 75, 66, and 44 kD) were identified. The specificity of spermidine binding was examined by gel-filtration competition experiments performed using other polyamines and compounds structurally related to spermidine. Partial purification on Sephadex G-200 led to the identification of 66- and 44-kD protein bands, which may represent the putative spermidine-binding protein(s) on the plasmalemma.

1   This work was supported in part by funds from the National Research Council of Italy, special project Ricerche Avanzate per Innovazioni nel Sistema Agricolo, subproject no. 2, and in part by funds from the Ministero dell'Università, della Ricerca Scientifica e Tecnologica. O.S. was a recipient of a grant from the Roche Research Foundation (Basel, Switzerland).
*   Corresponding author; e-mail bagninel{at}kaiser.alma.unibo.it; fax 39-51-242576.

Plant Physiol. (1998) 117: 971-977
Copyright Clearance Center:   0032-0889/98/117/0971/07
© 1998 American Society of Plant Physiologists




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