PMID:8530491
| Citation |
Nakai, M, Kinoshita, K and Endo, T (1995) Mitochondrial receptor complex protein. The intermembrane space domain of yeast MAS17 is not essential for its targeting or function. J. Biol. Chem. 270:30571-5 |
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| Abstract |
MAS17 (MAS22) is an essential component of the import receptor complex in the yeast mitochondrial outer membrane. MAS17 consists of three distinct domains: the N-terminal cytosolic domain, the internal membrane-spanning domain, and the C-terminal intermembrane space domain. In the present study, we examined the roles of the C-terminal domain of MAS17, which is rich in acidic amino acids, in protein import into mitochondria both in vivo and in vitro. Cells expressing MAS17 delta 120-152, a mutant MAS17 lacking the C-terminal acidic domain, could grow as fast as those expressing wild-type MAS17, while cells expressing MAS17 delta 97-152, a mutant MAS17 lacking both the intermembrane space and the membrane-spanning domains, stopped growing as soon as wild-type MAS17 was depleted. MAS17 delta 120-152 was correctly integrated into the mitochondrial outer membrane like wild-type MAS17. Mitochondria containing MAS17 delta 120-152 instead of wild-type MAS17 could import both authentic and artificial mitochondrial precursor proteins nearly as efficiently as wild-type mitochondria in vitro. These results suggest that the C-terminal intermembrane space domain of MAS17 is not essential for targeting or functions of MAS17. |
| Links | |
| Keywords |
Amino Acid Sequence; Animals; Fungal Proteins/biosynthesis; Fungal Proteins/chemistry; Fungal Proteins/metabolism; Intracellular Membranes/metabolism; Kinetics; Membrane Proteins; Membrane Transport Proteins; Mice; Mitochondria/metabolism; Mitochondrial Membrane Transport Proteins; Molecular Sequence Data; Mutagenesis, Insertional; Mutagenesis, Site-Directed; Point Mutation; Protein Biosynthesis; Protein Precursors/metabolism; Protein Processing, Post-Translational; Rabbits; Receptors, Cell Surface; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Reticulocytes/metabolism; Saccharomyces cerevisiae/growth & development; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship |
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