Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae
Echave Lozano, Pedro
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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.
Is part ofThe Journal of Biological Chemistry, 2002, vol. 277, núm 46, p. 44531-44538
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