title: Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon.
abstract: Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria. Cells lacking both proteins exhibit defects in respiration-dependent growth, degradation of mitochondrially synthesized proteins, and assembly of inner-membrane complexes. Defects in growth and protein assembly, but not in degradation, were suppressed by overproduction of yeast mitochondrial Lon, an ATP-dependent serine protease. Suppression by Lon was enhanced by inactivation of the proteolytic site and was prevented by mutation of the ATP-binding site. It is suggested that the mitochondrial proteases Lon, Afg3p, and Rca1p can also serve a chaperone-like function in the assembly of mitochondrial protein complexes.
authors.affiliation: Department of Molecular Cell Biology, University of Amsterdam, Kruislaan 318, 1098 SM Amsterdam, The Netherlands.
authors.forename: M
authors.initials: M
authors.lastname: Rep
authors.forename: J M
authors.initials: JM
authors.lastname: van Dijl
authors.forename: K
authors.initials: K
authors.lastname: Suda
authors.forename: G
authors.initials: G
authors.lastname: Schatz
authors.forename: L A
authors.initials: LA
authors.lastname: Grivell
authors.forename: C K
authors.initials: CK
authors.lastname: Suzuki
mesh_terms: D049069:ATP-Dependent Proteases; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003576:Electron Transport Complex IV / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008666:Metalloendopeptidases; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D006180:Proton-Translocating ATPases / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D029701:Saccharomyces cerevisiae Proteins; D000255:Adenosine Triphosphate; D003576:Electron Transport Complex IV; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; D008666:Metalloendopeptidases; D000251:Adenosine Triphosphatases; C102166:YTA12 protein, S cerevisiae; C090045:AFG3 protein, S cerevisiae; D006180:Proton-Translocating ATPases