The N-terminal 21 amino acids of a 70 kDa protein of the yeast mitochondrial outer membrane direct E. coli beta-galactosidase into the mitochondrial matrix space in yeast cells.
The intracellular location of fusion proteins was investigated in yeast cells. They consisted of the N-terminal 21, 61 or 292 amino acids of the 70 kDa protein of the yeast mitochondrial outer membrane and an enzymatically active E. coli beta-galactosidase. The hybrids containing 61 or 292 residues of the 70 kDa protein, as well as the original 70 kDa protein, were localized on the outer membrane in a tightly membrane-bound form. In contrast, the other hybrid was exclusively localized in the mitochondrial matrix space as a soluble protein.
Hase
T
T
Nakai
M
M
Matsubara
H
H
D003600:Cytosol / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D005656:Fungal Proteins / Q000378:metabolism*; D005696:Galactosidases / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism / Q000648:ultrastructure*; D014357:Trypsin / Q000494:pharmacology; D001616:beta-Galactosidase / Q000378:metabolism*
D005656:Fungal Proteins; D008565:Membrane Proteins; D005696:Galactosidases; D001616:beta-Galactosidase; D014357:Trypsin