Literature DB >> 9635430

The preprotein translocation channel of the outer membrane of mitochondria.

K P Künkele1, S Heins, M Dembowski, F E Nargang, R Benz, M Thieffry, J Walz, R Lill, S Nussberger, W Neupert.   

Abstract

The preprotein translocase of the outer membrane of mitochondria (TOM complex) facilitates the recognition, insertion, and translocation of nuclear-encoded mitochondrial preproteins. We have purified the TOM complex from Neurospora crassa and analyzed its composition and functional properties. The TOM complex contains a cation-selective high-conductance channel. Upon reconstitution into liposomes, it mediates integration of proteins into and translocation across the lipid bilayer. TOM complex particles have a diameter of about 138 A, as revealed by electron microscopy and image analysis; they contain two or three centers of stain-filled openings, which we interpret as pores with an apparent diameter of about 20 A. We conclude that the structure reported here represents the protein-conducting channel of the mitochondrial outer membrane.

Entities:  

Mesh:

Substances:

Year:  1998        PMID: 9635430     DOI: 10.1016/s0092-8674(00)81206-4

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  110 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.  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

3.  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

4.  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

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.  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

8.  The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria.

Authors:  N Wiedemann; N Pfanner; M T Ryan
Journal:  EMBO J       Date:  2001-03-01       Impact factor: 11.598

9.  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 10.  Signals and receptors--the translocation machinery on the mitochondrial surface.

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

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.