|
Título:
|
Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
|
|
Autor/a:
|
Cabiscol Català, Elisa; Piulats Combalia, Eva; Echave Lozano, Pedro; Herrero Perpiñán, Enrique; Ros Salvador, Joaquim
|
|
Notas:
|
We have analyzed the proteins that are oxidatively
damaged when Saccharomyces cerevisiae cells are ex-
posed to stressing conditions. Carbonyl groups generated
by hydrogen peroxide or menadione on proteins of aero-
bically respiring cells were detected by Western blotting,
purified, and identified. Mitochondrial proteins such as
E2 subunits of both pyruvate dehydrogenase and ␣-keto-
glutarate dehydrogenase, aconitase, heat-shock protein
60, and the cytosolic fatty acid synthase (␣ subunit) and
glyceraldehyde-3-phosphate dehydrogenase were the ma-
jor targets. In addition we also report the in vivo modifi-
cation of lipoamide present in the above-mentioned E2
subunits under the stressing conditions tested and that
this also occurs with the homologous enzymes present in
Escherichia coli cells that were used for comparative
analysis. Under fermentative conditions, the main pro-
tein targets in S. cerevisiae cells treated with hydrogen
peroxide or menadione were pyruvate decarboxylase,
enolase, fatty acid synthase, and glyceraldehyde-3-phos-
phate dehydrogenase. Under the stress conditions tested,
fermenting cells exhibit a lower viability than aerobically
respiring cells and, consistently, increased peroxide gen-
eration as well as higher content of protein carbonyls and
lipid peroxides. Our results strongly suggest that the
oxidative stress in prokaryotic and eukaryotic cells
shares common features. |
|
Derechos:
|
(c) The American Society for Biochemistry and Molecular Biology, 2000
|
|
Tipo de documento:
|
article
publishedVersion |
|
Editor:
|
The American Society for Biochemistry and Molecular Biology
|
|
Compartir:
|
|
