Literature DB >> 9442867

Mitochondrial preprotein translocase.

N Pfanner1, E A Craig, A Hönlinger.   

Abstract

Mitochondria import most of their proteins from the cytosol. Dynamic protein complexes in the mitochondrial outer and inner membranes are responsible for the specific recognition and membrane translocation of preproteins. The preprotein translocase of the outer mitochondrial membrane contains several import receptors and a general import pore. The preprotein translocase of the inner membrane consists of a channel interacting with preproteins in transit and an import motor that includes the matrix heat shock protein Hsp70. Acidic patches of import components are thought to guide the import of positively charged signal sequences (acid chain hypothesis). Energy input is derived from the inner membrane potential and ATP. Proteins in the mitochondrial matrix are required for proteolytic processing and folding of imported proteins. The dynamic nature of the membrane translocase permits sorting of preproteins at distinct stages of the import pathway.

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Year:  1997        PMID: 9442867     DOI: 10.1146/annurev.cellbio.13.1.25

Source DB:  PubMed          Journal:  Annu Rev Cell Dev Biol        ISSN: 1081-0706            Impact factor:   13.827


  44 in total

1.  An internal targeting signal directing proteins into the mitochondrial intermembrane space.

Authors:  K Diekert; G Kispal; B Guiard; R Lill
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-12       Impact factor: 11.205

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.  Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria.

Authors:  U Fünfschilling; S Rospert
Journal:  Mol Biol Cell       Date:  1999-10       Impact factor: 4.138

4.  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 5.  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

6.  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

7.  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

8.  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

9.  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

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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