Literature DB >> 8530491

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

M Nakai1, K Kinoshita, T Endo.   

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.

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Year:  1995        PMID: 8530491     DOI: 10.1074/jbc.270.51.30571

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  14 in total

1.  Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane.

Authors:  T Kanamori; S Nishikawa; M Nakai; I Shin; P G Schultz; T Endo
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-30       Impact factor: 11.205

Review 2.  Signals and receptors--the translocation machinery on the mitochondrial surface.

Authors:  E Schleiff
Journal:  J Bioenerg Biomembr       Date:  2000-02       Impact factor: 2.945

3.  Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40.

Authors:  Koji Yamano; Sachiko Tanaka-Yamano; Toshiya Endo
Journal:  J Biol Chem       Date:  2010-10-29       Impact factor: 5.157

4.  Role of the negative charges in the cytosolic domain of TOM22 in the import of precursor proteins into mitochondria.

Authors:  F E Nargang; D Rapaport; R G Ritzel; W Neupert; R Lill
Journal:  Mol Cell Biol       Date:  1998-06       Impact factor: 4.272

5.  Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex.

Authors:  P J Dekker; M T Ryan; J Brix; H Müller; A Hönlinger; N Pfanner
Journal:  Mol Cell Biol       Date:  1998-11       Impact factor: 4.272

6.  Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis.

Authors:  T Komiya; S Rospert; C Koehler; R Looser; G Schatz; K Mihara
Journal:  EMBO J       Date:  1998-07-15       Impact factor: 11.598

7.  Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria.

Authors:  D A Court; F E Nargang; H Steiner; R S Hodges; W Neupert; R Lill
Journal:  Mol Cell Biol       Date:  1996-08       Impact factor: 4.272

8.  The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences.

Authors:  M Moczko; U Bömer; M Kübrich; N Zufall; A Hönlinger; N Pfanner
Journal:  Mol Cell Biol       Date:  1997-11       Impact factor: 4.272

Review 9.  The mitochondrial protein import pathway: are precursors imported through membrane channels?

Authors:  R E Jensen; K W Kinnally
Journal:  J Bioenerg Biomembr       Date:  1997-02       Impact factor: 2.945

Review 10.  The first steps of protein import into mitochondria.

Authors:  V Haucke; T Lithgow
Journal:  J Bioenerg Biomembr       Date:  1997-02       Impact factor: 2.945

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