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Science 8 April 1994:
Vol. 264. no. 5156, pp. 273 - 276
DOI: 10.1126/science.8146662
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Articles

Science, Vol 264, Issue 5156, 273-276
Copyright © 1994 by American Association for the Advancement of Science

articles

Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration

CK Suzuki, K Suda, N Wang, and G Schatz

Biozentrum der Universitat Basel, Switzerland.

The role of protein degradation in mitochondrial homeostasis was explored by cloning of a gene from Saccharomyces cerevisiae that encodes a protein resembling the adenosine triphosphate (ATP)-dependent bacterial protease Lon. The predicted yeast protein has a typical mitochondrial matrix-targeting sequence at its amino terminus. Yeast cells lacking a functional LON gene contained a nonfunctional mitochondrial genome, were respiratory-deficient, and lacked an ATP-dependent proteolytic activity present in the mitochondria of Lon+ cells. Lon- cells were also impaired in their ability to catalyze the energy-dependent degradation of several mitochondrial matrix proteins and they accumulated electron-dense inclusions in their mitochondrial matrix.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Roles for the Human ATP-dependent Lon Protease in Mitochondrial DNA Maintenance.
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Multiple Intracellular Locations of Lon Protease in Arabidopsis: Evidence for the Localization of AtLon4 to Chloroplasts.
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Cleavage Site Selection within a Folded Substrate by the ATP-dependent Lon Protease.
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The ClpB Homolog Hsp78 Is Required for the Efficient Degradation of Proteins in the Mitochondrial Matrix.
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J. Biol. Chem. 277, 45829-45837
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Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease.
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Functional Proteolytic Complexes of the Human Mitochondrial ATP-dependent Protease, hClpXP.
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Peripheral Mitochondrial Inner Membrane Protein, Mss2p, Required for Export of the Mitochondrially Coded Cox2p C Tail in Saccharomyces cerevisiae.
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Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits.
H. Stahlberg, E. Kutejova, K. Suda, B. Wolpensinger, A. Lustig, G. Schatz, A. Engel, and C. K. Suzuki (1999)
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Substrate sequestration by a proteolytically inactive Lon mutant.
L. Van Melderen and S. Gottesman (1999)
PNAS 96, 6064-6071
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Higher Plant Mitochondria.
S. Mackenzie and L. McIntosh (1999)
PLANT CELL 11, 571-586
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A Novel DNA-Binding Protein Bound to the Mitochondrial Inner Membrane Restores the Null Mutation of Mitochondrial Histone Abf2p in Saccharomyces cerevisiae.
J. H. Cho, S. J. Ha, L. R. Kao, T. L. Megraw, and C.-B. Chae (1998)
Mol. Cell. Biol. 18, 5712-5723
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The ATPase and protease domains of yeast mitochondrial Lon: Roles in proteolysis and respiration-dependent growth.
J. M. van Dijl, E. Kutejova, K. Suda, G. Schatz, and C. K. Suzuki (1998)
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Protein quality control: triage by chaperones and proteases..
S Gottesman, S Wickner, and M R Maurizi (1997)
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Bacterial Protease Lon Is a Site-specific DNA-binding Protein.
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Caulobacter Lon protease has a critical role in cell-cycle control of DNA methylation..
R Wright, C Stephens, G Zweiger, L Shapiro, and M R Alley (1996)
Genes & Dev. 10, 1532-1542
   Abstract »    PDF »
Substitution of PIM1 Protease in Mitochondria by Escherichia coli Lon Protease.
U. Teichmann, L. van Dyck, B. Guiard, H. Fischer, R. Glockshuber, W. Neupert, and T. Langer (1996)
J. Biol. Chem. 271, 10137-10142
   Abstract »    Full Text »    PDF »
Degradation of Cytochrome Oxidase Subunits in Mutants of Yeast Lacking Cytochrome c and Suppression of the Degradation by Mutation of yme1.
D. A. Pearce and F. Sherman (1995)
J. Biol. Chem. 270, 20879-20882
   Abstract »    Full Text »    PDF »
Selective, Energy-dependent Proteolysis in Escherichia coli.
S. Gottesman, S. Wickner, Y. Yubete, S.K. Singh, M. Kessel, and M. Maurizi (1995)
Cold Spring Harb Symp Quant Biol 60, 533-548
   Abstract »    PDF »


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