ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae.
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.
Van Dyck
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Institut für Physiologische Chemie, Ludwig-Maximilians-Universität München, Germany.
Langer
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D049069:ATP-Dependent Proteases; D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D051545:Cyclooxygenase 1; D004579:Electron Transport / Q000235:genetics; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016678:Genome; D007527:Isoenzymes / Q000096:biosynthesis / Q000235:genetics; D008666:Metalloendopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones / Q000378:metabolism; D008969:Molecular Sequence Data; D011451:Prostaglandin-Endoperoxide Synthases / Q000096:biosynthesis / Q000235:genetics; D012326:RNA Splicing / Q000235:genetics; D020871:RNA Stability; D012194:RNA-Directed DNA Polymerase / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D007527:Isoenzymes; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; D000255:Adenosine Triphosphate; D051545:Cyclooxygenase 1; D011451:Prostaglandin-Endoperoxide Synthases; C066564:aI2 protein, S cerevisiae; D012194:RNA-Directed DNA Polymerase; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; C085155:PIM1 protein, S cerevisiae; D012697:Serine Endopeptidases; C082702:YME1 protein, S cerevisiae; D008666:Metalloendopeptidases; C114583:m-AAA proteases; D000251:Adenosine Triphosphatases