Fungal auxin antagonist hypaphorine competitively inhibits indole-3-acetic acid-dependent superoxide generation by horseradish peroxidase. |
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Authors: | T Kawano N Kawano H Hosoya F Lapeyrie |
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Affiliation: | Unité Mixte de Recherche INRA-UHP Interactions Arbres/Micro-organismes, Institut National de la Recherche Agronomique, Champenoux, F-54280, France. |
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Abstract: | Plant peroxidases (EC 1.11.1.7) including horseradish peroxidase (HRP-C), but not the nonplant peroxidases, are known to be highly specific indole-3-acetic acid (IAA) oxygenases which oxidize IAA in the absence of H2O2, and superoxide anion radicals (O2*-) are produced as by-products. Hypaphorine, a putative auxin antagonist isolated from ectomycorrhizal fungi, inhibited the IAA-dependent generation of O2*- by HRP-C, which occurs in the absence of H2O2. Hypaphorine has no effect on the nonspecific heme-catalyzed O2*- generation induced by high concentration of ethanol. It is probable that the inhibitory effect of hypaphorine on O2*- generation is highly specific to the IAA-dependent reaction. The mode of inhibition of the IAA-dependent O2*--generating reaction by hypaphorine was analyzed with a double-reciprocal plot and determined to be competitive inhibition, indicating that hypaphorine competes with IAA by binding to the putative IAA binding site on HRP-C. This implies the importance of structural similarity between hypaphorine and IAA. This work presented the first evidence for antagonism between IAA and a structurally related fungal alkaloid on binding to a purified protein which shares some structural similarity with auxin-binding proteins. |
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