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The N‐terminal 21 amino acids of a 70 kDa protein of the yeast mitochondrial outer membrane direct E. coli β‐galactosidase into the mitochondrial matrix space in yeast cells
Author(s) -
Hase Toshiharu,
Nakai Masato,
Matsubara Hiroshi
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80326-x
Subject(s) - yeast , translocase of the outer membrane , bacterial outer membrane , translocase of the inner membrane , mitochondrial carrier , biochemistry , mitochondrial matrix , inner mitochondrial membrane , fusion protein , mitochondrion , saccharomyces cerevisiae , chemistry , mitochondrial membrane transport protein , biology , cytosol , escherichia coli , recombinant dna , enzyme , gene
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 β‐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.