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Schlagwörter:
ATP-Dependent Proteases
Adenosine Triphosphatases/chemistry/genetics/metabolism
Adenosine Triphosphate/*metabolism
Amino Acid Sequence
Animals
Cyclooxygenase 1
Electron Transport/genetics
Endopeptidases/chemistry/genetics/*metabolism
Genome
Isoenzymes/biosynthesis/genetics
Metalloendopeptidases/chemistry/genetics/metabolism
Mitochondria/*enzymology/genetics/metabolism
Mitochondrial Proteins
Molecular Chaperones/metabolism
Molecular Sequence Data
Prostaglandin-Endoperoxide Synthases/biosynthesis/genetics
RNA Splicing/genetics
RNA Stability
RNA-Directed DNA Polymerase/genetics/metabolism
Saccharomyces cerevisiae/cytology/*enzymology/genetics/metabolism
*Saccharomyces cerevisiae Proteins
Serine Endopeptidases/chemistry/metabolism
Substrate Specificity
Zusammenfassung:
Regulated protein degradation by ATP-dependent proteases plays a fundamental role in the biogenesis of mitochondria. Membrane-bound and soluble ATP-dependent proteases have been identified in various subcompartments of this organelle. Subunits composing these proteases are evolutionarily conserved from yeast to humans and, in support of an endosymbiotic origin of mitochondria, evolved from prokaryotic ancestors: the PIM1/Lon protease is active in the matrix of mitochondria, while the i-AAA protease and the m-AAA protease mediate the turnover of inner membrane proteins. Most of the knowledge concerning the biogenesis and the physiological role of ATP-dependent proteases comes from studies in the yeast Saccharomyces cerevisiae. Proteases were found to be required for mitochondrial stasis, for the maintenance of the morphology of the organelle and for mitochondrial genome integrity. ATP-dependent proteolysis is crucial for the expression of mitochondrially encoded subunits of respiratory chain complexes and for the assembly of these complexes. Hence, mitochondrial ATP-dependent proteases exert multiple roles which are essential for the maintenance of cellular respiratory competence.
