PMID:8810243

Citation	Rep, M, van Dijl, JM, Suda, K, Schatz, G, Grivell, LA and Suzuki, CK (1996) Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon. Science 274:103-6
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.
Links	PubMed
Keywords	ATP-Dependent Proteases; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Base Sequence; Binding Sites; Electron Transport Complex IV/metabolism; Fungal Proteins/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Membrane Proteins/metabolism; Metalloendopeptidases; Mitochondria/metabolism; Mitochondrial Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Proton-Translocating ATPases/metabolism; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/growth & development; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism
edit table

Annotations

Gene product	Qualifier	GO ID	GO term name	Evidence Code	with/from	Aspect	Notes	Status
edit table

References

See Help:References for how to manage references in GONUTS.