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J. Biol. Chem., Vol. 276, Issue 49, 46284-46289, December 7, 2001

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Vesicle-associated Membrane Protein of Arabidopsis Suppresses Bax-induced Apoptosis in Yeast Downstream of Oxidative Burst^*

Alex Levine^§¶, Beatrice Belenghi^§, Hila Damari-Weisler, and David Granot

From the  Department of Plant Sciences, The Hebrew University of Jerusalem, Givat-Ram, Jerusalem 91904, Israel and the  Institute of Field and Garden Crops, Agricultural Research Organization, The Volcani Center, Bet-Dagan 50250, Israel

Programmed cell death (PCD) in many systems is controlled by relative amounts of the apoptosis-regulating proteins Bax and Bcl-2 through homo- or heterodimerization. Here we show that Bax-induced PCD of yeast was suppressed by transformation with a vesicle-associated membrane protein from Arabidopsis (AtVAMP), which was isolated by screening a cDNA expression library against sugar-induced cell death in yeast. AtVAMP expression blocked Bax-induced PCD downstream of oxidative burst. AtVAMP also prevented H₂O₂-induced apoptosis in yeast and in Arabidopsis cells. Reduced oxidation of lipids and plasma membrane proteins was detected in the AtVAMP-transformed yeast, suggesting improved membrane repair. Inhibition of intracellular vesicle trafficking by brefeldin A induced apoptosis from a sublethal concentration of H₂O₂. No protection occurred by overexpression of the yeast homolog SCN2. However, efficient suppression of yeast PCD occurred by expression of a chimeric gene, composed of the conserved domains from yeast, fused to the variable N-terminal domain from Arabidopsis, resulting in exchange of the proline-rich N-terminal domain of SCN2 with a proline-poor Arabidopsis sequence. Our results suggest that intracellular vesicle traffic can regulate execution of apoptosis by affecting the rate of membrane recycling and that the proline-rich N-terminal domain of VAMP inhibited this process.

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