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PMID: 3081371 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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.

FEBS letters ·Vol. 197 ·No. 1-2 ·1986-03-03 ·Pages 199-203

Hase T, Nakai M, Matsubara H

Abstract

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.

MeSH Terms
Cytosol/metabolism Escherichia coli/enzymology Fungal Proteins/metabolism Galactosidases/metabolism Intracellular Membranes/metabolism Membrane Proteins/metabolism Mitochondria/metabolism Saccharomyces cerevisiae/metabolism,ultrastructure Trypsin/pharmacology beta-Galactosidase/metabolism
Chemicals
Fungal Proteins Membrane Proteins Galactosidases beta-Galactosidase Trypsin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hase T
Nakai M
Matsubara H
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1986-03-03
Pages
199-203
Language
English
Region
England
NLM ID
0155157
Subset
IM
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