Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae

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2002Author
Echave Lozano, Pedro
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Cabiscol Català, Elisa;
Bellí i Martínez, Gemma;
Tamarit Sumalla, Jordi;
Echave Lozano, Pedro;
Herrero Perpiñán, Enrique;
Ros Salvador, Joaquim;
.
(2002)
.
Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae.
The Journal of Biological Chemistry, 2002, vol. 277, núm 46, p. 44531-44538.
https://doi.org/10.1074/jbc.M206525200.
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Show full item recordAbstract
In the present study, we have analyzed the role of the
molecular chaperone Hsp60 in protection of Saccharo-
myces cerevisiae against oxidative damage. We con-
structed mutant strains in which the levels of Hsp60
protein, compared with wild-type cells, were four times
greater, and the addition of doxycycline gradually re-
duces them to 20% of wild-type. Under oxidative-stress
conditions, the progressive decrease in Hsp60 levels in
these mutants resulted in reduced cell viability and an
increase in both cell peroxide species and protein car-
bonyl content. Protection of Fe/S-containing enzymes
from oxidative inactivation was found to be dose-de-
pendent with respect to Hsp60 levels. As these enzymes
release their iron ions under oxidative-stress condi-
tions, the intracellular labile iron pool, monitored with
calcein, was higher in cells with reduced Hsp60 levels.
Consistently, the iron chelator deferoxamine protected
low Hsp60-expressing cells from both oxidant-induced
death and protein oxidation. These results indicate that
the role of Hsp60 in oxidative-stress defense is explained
by protection of several Fe/S proteins, which prevent
the release of iron ions and thereby avert further
damage.
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The Journal of Biological Chemistry, 2002, vol. 277, núm 46, p. 44531-44538European research projects
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