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Plant Physiol, August 2002, Vol. 129, pp. 1908-1920
Transgenic Plant Cells Lacking Mitochondrial Alternative Oxidase
Have Increased Susceptibility to Mitochondria-Dependent and
-Independent Pathways of Programmed Cell Death1
Christine A.
Robson and
Greg C.
Vanlerberghe*
Division of Life Sciences and Department of Botany, University of
Toronto at Scarborough, 1265 Military Trail, Scarborough, Ontario,
Canada M1C 1A4
The plant mitochondrial electron transport chain is branched such
that electrons at ubiquinol can be diverted to oxygen via the
alternative oxidase (AOX). This pathway does not contribute to ATP
synthesis but can dampen the mitochondrial generation of reactive
oxygen species. Here, we establish that transgenic tobacco (Nicotiana tabacum L. cv Petit Havana SR1) cells lacking
AOX (AS8 cells) show increased susceptibility to three different
death-inducing compounds (H2O2, salicylic acid
[SA], and the protein phosphatase inhibitor cantharidin) in
comparison with wild-type cells. The timing and extent of AS8 cell
death are very similar among the three treatments and, in each case,
are accompanied by the accumulation of oligonucleosomal fragments of
DNA, indicative of programmed cell death. Death induced by
H2O2 or SA occurs by a mitochondria-dependent pathway characterized by cytochrome c release from the mitochondrion. Conversely, death induced by cantharidin occurs by a pathway without any obvious mitochondrial involvement. The ability of AOX to attenuate these death pathways may relate to its ability to maintain
mitochondrial function after insult with a death-inducing compound or
may relate to its ability to prevent chronic oxidative stress within
the mitochondrion. In support of the latter, long-term treatment of AS8
cells with an antioxidant compound increased the resistance of AS8
cells to SA- or cantharidin-induced death. The results indicate that
plants maintain both mitochondria-dependent and -independent pathways
of programmed cell death and that AOX may act as an important
mitochondrial "survival protein" against such death.
1
This work was supported by a grant from the
Natural Sciences and Engineering Research Council of Canada and by a
Premiers Research Excellence Award of Ontario (both to G.C.V.).
*
Corresponding author; e-mail gregv{at}utsc.utoronto.ca; fax
416-287-7642.
© 2002 American Society of Plant Physiologists
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