Import of proteins into yeast mitochondria: the purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes.
We have purified the metalloprotease which is localized in the soluble matrix space of Saccharomyces cerevisiae mitochondria and cleaves the amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins. The enzyme consists of two loosely associated non-identical subunits of mol. wt 48,000 and 51,000, respectively. Attempts to separate the two subunits from each other caused loss of activity. The smaller subunit had been identified as the product of the nuclear MAS1 gene (Witte et al., 1988). The larger subunit is now identified as the product of the nuclear MAS2 gene.
Yang
M
M
Biocenter, University of Basel, Switzerland.
Jensen
R E
RE
Yaffe
M P
MP
Oppliger
W
W
Schatz
G
G
D000426:Alcohol Dehydrogenase / Q000378:metabolism; D015153:Blotting, Western; D003574:Cytochrome c Group / Q000378:metabolism; D004271:DNA, Fungal / Q000235:genetics; D003576:Electron Transport Complex IV / Q000378:metabolism; D005800:Genes, Fungal; D008666:Metalloendopeptidases / Q000235:genetics* / Q000302:isolation & purification; D008928:Mitochondria / Q000201:enzymology*; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D006180:Proton-Translocating ATPases / Q000378:metabolism; D012441:Saccharomyces cerevisiae
D003574:Cytochrome c Group; D004271:DNA, Fungal; D011498:Protein Precursors; D000426:Alcohol Dehydrogenase; D003576:Electron Transport Complex IV; D008666:Metalloendopeptidases; D006180:Proton-Translocating ATPases