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PMID: 8530491 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Mitochondrial receptor complex protein. The intermembrane space domain of yeast MAS17 is not essential for its targeting or function.

The Journal of biological chemistry ·Vol. 270 ·No. 51 ·1995-12-22 ·Pages 30571-5

Nakai M, Kinoshita K, Endo T

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.

MeSH Terms
Amino Acid Sequence Animals Fungal Proteins/biosynthesis,chemistry,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,chemistry,metabolism Reticulocytes/metabolism Saccharomyces cerevisiae/growth & development,metabolism Saccharomyces cerevisiae Proteins Structure-Activity Relationship
Chemicals
Fungal Proteins Membrane Proteins Membrane Transport Proteins Mitochondrial Membrane Transport Proteins Protein Precursors Receptors, Cell Surface Recombinant Proteins Saccharomyces cerevisiae Proteins TOM22 protein, S cerevisiae
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Nakai M
Department of Chemistry, Faculty of Science, Nagoya University, Japan.
Kinoshita K
Endo T
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1995-12-22
Pages
30571-5
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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