Autori: Daniela A. Bota, Kelvin J.A. Davies

Editorial: nature, Nature Cell Biology, 4, p.674-680, 2002.

Rezumat:

Mitochondrial aconitase is sensitive to oxidative inactivation and can aggregate and accumulate in various age-related disorders. We now report that the ATP-stimulated, mitochondrial-matrix, „Lon” protease selectively recognizes and degrades the oxidized, hydrophobic form of aconitase after mild oxidative modification but severe oxidation results in aconitase aggregation, which makes it a poor Lon substrate. Similarly, a morpholino oligodeoxynucleotide directed against the lon gene dramatically decreased Lon protein levels, Lon activity, and aconitase degradation in WI-38 VA-13 human lung fibroblasts, and caused accumulation of oxidatively modified aconitase. The ATP-stimulated Lon protease may be an essential defense against the stress of life in an oxygen environment. By recognizing minor oxidative changes to aconitase structure, and rapidly degrading the mildly modified protein, the Lon protease may prevent extensive oxidation, aggregation, and accumulation, which could otherwise compromise mitochondrial function and cellular viability. Aconitase is probably only one of many mitochondrial matrix proteins that are preferentially degraded by Lon following oxidative modification.

Cuvinte cheie: Aconitase, Proteaza Lon // Aconitase, Lon Protease

URL: http://www.nature.com/naturecellbiology