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Vesicle-associated Membrane Protein of Arabidopsis Suppresses Bax-induced Apoptosis in Yeast Downstream of Oxidative Burst
Year:
2001
Source of publication :
Journal of Biological Chemistry
Authors :
Damari-Weissler, Hila
;
.
Granot, David
;
.
Volume :
276
Co-Authors:
Levine, A., Department of Plant Sciences, Hebrew University of Jerusalem, Givat-Ram, Jerusalem 91904, Israel
Belenghi, B., Department of Plant Sciences, Hebrew University of Jerusalem, Givat-Ram, Jerusalem 91904, Israel
Damari-Weisler, H., Institute of Field and Garden Crops, Agricultural Research Organization, Volcani Center, Bet-Dagan 50250, Israel
Granot, D., Institute of Field and Garden Crops, Agricultural Research Organization, Volcani Center, Bet-Dagan 50250, Israel
Facilitators :
From page:
46284
To page:
46289
(
Total pages:
6
)
Abstract:
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 H2O 2-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.
Note:
Related Files :
apoptosis
arabidopsis
DNA
Lipids
proteins
reactive oxygen species
recycling
Yeast
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More details
DOI :
10.1074/jbc.M107375200
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
19727
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:31
Scientific Publication
Vesicle-associated Membrane Protein of Arabidopsis Suppresses Bax-induced Apoptosis in Yeast Downstream of Oxidative Burst
276
Levine, A., Department of Plant Sciences, Hebrew University of Jerusalem, Givat-Ram, Jerusalem 91904, Israel
Belenghi, B., Department of Plant Sciences, Hebrew University of Jerusalem, Givat-Ram, Jerusalem 91904, Israel
Damari-Weisler, H., Institute of Field and Garden Crops, Agricultural Research Organization, Volcani Center, Bet-Dagan 50250, Israel
Granot, D., Institute of Field and Garden Crops, Agricultural Research Organization, Volcani Center, Bet-Dagan 50250, Israel
Vesicle-associated Membrane Protein of Arabidopsis Suppresses Bax-induced Apoptosis in Yeast Downstream of Oxidative Burst
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 H2O 2-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.
Scientific Publication
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