Abstract

Stimulation of G-protein activity by the amphipathic tetradecapeptide mastoparan is well documented in animal systems and occurs via mimickry of the third cytoplasmic domain of the cognate seven-transmembrane-span (7TMS) receptor. Binding of guanosine 5′-O-thiotriphosphate to microsomal and plasma-membrane fractions from Pisum sativum L. and Zea mays L. was stimulated by the tetradecapeptide mastoparan analogue mas 7 over a narrow concentration range, with maximal effect exerted at 10 μM peptide, while the nonamphipathic analogue, mas CP, which differed from mas 7 by only one amino acid, was ineffective at promoting binding. This stimulation could be completely abolished by inclusion of low concentrations of the non-ionic detergents nonanoyl-N-methylglucamide and Lubrol PX. Taken together, these data provide good evidence for the existence of G-protein-linked 7TMS receptors in higher plant systems.

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