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Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism

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Bota, Daniela A., Davies, Kelvin J. A.·2002·Nature Cell Biology

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Abstract

Mitochondrial aconitase is sensitive to oxidative inactivation and can aggregate and accumulate in many age-related disorders. Here we report that Lon protease, an ATP-stimulated mitochondrial matrix protein, selectively recognizes and degrades the oxidized, hydrophobic form of aconitase after mild oxidative modification, but that severe oxidation results in aconitase aggregation, which makes it a poor substrate for Lon. Similarly, a morpholino oligodeoxynucleotide directed against the lon gene markedly decreases the amount of Lon protein, Lon activity and aconitase degradation in WI-38 VA-13 human lung fibroblasts and causes accumulation of oxidatively modified aconitase. The ATP-stimulated Lon protease may be an essential defence against the stress of life in an oxygen environment. By recognizing minor oxidative changes to protein structure and rapidly degrading the mildly modified protein, Lon protease may prevent extensive oxidation, aggregation and accumulation of aconitase, 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 protease after oxidative modification.

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Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Protein Oxidation in Aging, Disease, and Oxidative Stress
Berlett, B. S., & Stadtman, E. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20313 · Cited by 3,379
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Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010
Self-citation
Purification and properties
Cox, B. M., Opheim, K. E., Teschemacher, H., & D, A. G. M. (1975) · Life Sciences · doi:10.1016/0024-3205(75)90272-6 · Cited by 1,708
Gene expression profile of aging and its retardation by caloric restriction
Lee, C.-K., Klopp, R. G., Weindruch, R., & Prolla, T. A. (1999) · Science · doi:10.1126/science.285.5432.1390 · Cited by 1,473
Morpholino Antisense Oligomers: Design, Preparation, and Properties
Summerton, J. E., & Weller, D. D. (1997) · Antisense and Nucleic Acid Drug Development · doi:10.1089/oli.1.1997.7.187 · Cited by 1,137
Degradation of oxidized proteins in mammalian cells
Grune, T., Reinheckel, T., & Davies, K. J. A. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.7.9212076 · Cited by 835
Self-citation
Labeling of proteins by reductive methylation using sodium cyanoborohydride.
Jentoft, N., & Dearborn, D. G. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30016-9 · Cited by 771
[42]Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines
Trounce, I. A., Kim, Y. L., Jun, A. S., & Wallace, D. C. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64044-0 · Cited by 749
The oxidative inactivation of mitochondrial electron transport chain components and ATPase.
Zhang, Y., Marcillat, O., Giulivi, C., Ernster, L., & Davies, K. J. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46227-2 · Cited by 719
Self-citation

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Authors: Bota, D. A., & Davies, K. J. A.
Affiliations: University of Southern California (US)
Corresponding author: Davies, Kelvin J. A.
ORCID: Bota, Daniela A.
Davies, Kelvin J. A.
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2002-08-27
Volume: 4
Issue: 9
Pages: 674-680
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb836
OpenAlex: W2036284918
Cited by: 557
References: 53
Citations by year: 2026: 15 · 2025: 21 · 2024: 15 · 2023: 19 · 2022: 21 · 2021: 21 · 2020: 21 · 2019: 18 · 2018: 32 · 2017: 26 · 2016: 24 · 2015: 25 · 2014: 25 · 2013: 31 · 2012: 45
FWCI: 4.12
Type: journal article
Language: en
Open access: green
escholarship.org
Licence: cc-by
www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
eScholarship (California Digital Library) (submittedVersion, cc-by)
Funders: National Institutes of Health
National Institute on Aging (R01AG016256, AG16256)
National Institute of Environmental Health Sciences (ES03598)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords: Lon protease, mitochondrial aconitase, protein oxidation, protein degradation, protein aggregation, mitochondrial matrix, oxidative stress, age-related diseases, WI-38 fibroblasts, mitochondrial function
MeSH terms: Aconitate Hydratase, Adenosine Triphosphate, Animals, Base Sequence, Cattle, Cell Line, Heat-Shock Proteins, Humans, Hydrogen Peroxide, Kinetics, Mitochondria, Mitochondria, Heart, Oxidation-Reduction, Serine Endopeptidases, Oligodeoxyribonucleotides, Antisense, ATP-Dependent Proteases, In Vitro Techniques

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Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism

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