Literature DB >> 9242927

Protein import into mitochondria.

W Neupert1.   

Abstract

Mitochondria import many hundreds of different proteins that are encoded by nuclear genes. These proteins are targeted to the mitochondria, translocated through the mitochondrial membranes, and sorted to the different mitochondrial subcompartments. Separate translocases in the mitochondrial outer membrane (TOM complex) and in the inner membrane (TIM complex) facilitate recognition of preproteins and transport across the two membranes. Factors in the cytosol assist in targeting of preproteins. Protein components in the matrix partake in energetically driving translocation in a reaction that depends on the membrane potential and matrix-ATP. Molecular chaperones in the matrix exert multiple functions in translocation, sorting, folding, and assembly of newly imported proteins.

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Year:  1997        PMID: 9242927     DOI: 10.1146/annurev.biochem.66.1.863

Source DB:  PubMed          Journal:  Annu Rev Biochem        ISSN: 0066-4154            Impact factor:   23.643


  293 in total

1.  Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex.

Authors:  M Endres; W Neupert; M Brunner
Journal:  EMBO J       Date:  1999-06-15       Impact factor: 11.598

2.  Two distinct mechanisms drive protein translocation across the mitochondrial outer membrane in the late step of the cytochrome b(2) import pathway.

Authors:  M Esaki; T Kanamori; S i Nishikawa; T Endo
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-12       Impact factor: 11.205

3.  Protein import into plant mitochondria: precursor proteins differ in ATP and membrane potential requirements.

Authors:  M Tanudji; P Dessi; M Murcha; J Whelan
Journal:  Plant Mol Biol       Date:  2001-02       Impact factor: 4.076

Review 4.  Protein unfolding by mitochondria. The Hsp70 import motor.

Authors:  A Matouschek; N Pfanner; W Voos
Journal:  EMBO Rep       Date:  2000-11       Impact factor: 8.807

5.  Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small tom proteins, and import receptors.

Authors:  C Meisinger; M T Ryan; K Hill; K Model; J H Lim; A Sickmann; H Müller; H E Meyer; R Wagner; N Pfanner
Journal:  Mol Cell Biol       Date:  2001-04       Impact factor: 4.272

6.  Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathway.

Authors:  M Kurz; H Martin; J Rassow; N Pfanner; M T Ryan
Journal:  Mol Biol Cell       Date:  1999-07       Impact factor: 4.138

7.  Chemical cleavage of the overexpressed mitochondrial F1beta precursor with CNBr: a new strategy to construct an import-competent preprotein.

Authors:  P F Pavlov; P Moberg; X P Zhang; E Glaser
Journal:  Biochem J       Date:  1999-07-01       Impact factor: 3.857

8.  The precursor of the F1beta subunit of the ATP synthase is covalently modified upon binding to plant mitochondrial.

Authors:  E von Stedingk; P F Pavlov; V A Grinkevich; E Glaser
Journal:  Plant Mol Biol       Date:  1999-11       Impact factor: 4.076

9.  Toc34 is a preprotein receptor regulated by GTP and phosphorylation.

Authors:  N Sveshnikova; J Soll; E Schleiff
Journal:  Proc Natl Acad Sci U S A       Date:  2000-04-25       Impact factor: 11.205

10.  The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.

Authors:  J H Lim; F Martin; B Guiard; N Pfanner; W Voos
Journal:  EMBO J       Date:  2001-03-01       Impact factor: 11.598

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