Literature DB >> 1657948

Protein import into the yeast mitochondrial matrix. A new translocation intermediate between the two mitochondrial membranes.

S T Hwang1, C Wachter, G Schatz.   

Abstract

Import of authentic or artificial precursor proteins into the matrix of isolated yeast mitochondria can proceed via a translocation intermediate that is lodged between the two mitochondrial membranes. The intermediate accumulates when import is arrested by depleting mitochondria of ATP. Generation of the intermediate requires a potential across the inner membrane. The intermediate is membrane-bound, partly or completely processed (depending on the precursor), and chased into the matrix by added ATP. This chase does not require a potential across the inner membrane. The properties of this intermediate support the proposal (Hwang, S., Jascur, J., Vestweber, D., Pon, L., and Schatz, G. (1989) J. Cell Biol. 109, 487-493) that import into the matrix involves two distinct translocation systems in the outer and the inner mitochondrial membrane that are not permanently coupled to each other. Only translocation across the inner membrane requires ATP in the matrix.

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Year:  1991        PMID: 1657948

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


  26 in total

1.  Models of post-translational protein translocation.

Authors:  T C Elston
Journal:  Biophys J       Date:  2000-11       Impact factor: 4.033

2.  Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane.

Authors:  P E Scherer; U C Manning-Krieg; P Jenö; G Schatz; M Horst
Journal:  Proc Natl Acad Sci U S A       Date:  1992-12-15       Impact factor: 11.205

3.  The dimensions of the protein import channels in the outer and inner mitochondrial membranes.

Authors:  M P Schwartz; A Matouschek
Journal:  Proc Natl Acad Sci U S A       Date:  1999-11-09       Impact factor: 11.205

4.  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

5.  Strong precursor-pore interactions constrain models for mitochondrial protein import.

Authors:  J F Chauwin; G Oster; B S Glick
Journal:  Biophys J       Date:  1998-04       Impact factor: 4.033

6.  In vivo zippering of inner and outer mitochondrial membranes by a stable translocation intermediate.

Authors:  N Schülke; N B Sepuri; D Pain
Journal:  Proc Natl Acad Sci U S A       Date:  1997-07-08       Impact factor: 11.205

7.  Adaptation of a Genetic Screen Reveals an Inhibitor for Mitochondrial Protein Import Component Tim44.

Authors:  Non Miyata; Zhiye Tang; Michael A Conti; Meghan E Johnson; Colin J Douglas; Samuel A Hasson; Robert Damoiseaux; Chia-En A Chang; Carla M Koehler
Journal:  J Biol Chem       Date:  2017-02-06       Impact factor: 5.157

8.  Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria.

Authors:  V Haucke; C S Ocana; A Hönlinger; K Tokatlidis; N Pfanner; G Schatz
Journal:  Mol Cell Biol       Date:  1997-07       Impact factor: 4.272

Review 9.  Genetic and biochemical dissection of the mitochondrial protein-import machinery.

Authors:  M Kübrich; K Dietmeier; N Pfanner
Journal:  Curr Genet       Date:  1995-04       Impact factor: 3.886

10.  Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins.

Authors:  U Bömer; A C Maarse; F Martin; A Geissler; A Merlin; B Schönfisch; M Meijer; N Pfanner; J Rassow
Journal:  EMBO J       Date:  1998-08-03       Impact factor: 11.598

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