Document Detail

Reconstitution of import-competent outer membrane vesicles from mammalian mitochondria.
MedLine Citation:
PMID:  7798173     Owner:  NLM     Status:  MEDLINE    
Protein insertion into mitochondrial outer membrane (OM) vesicles isolated from Neurospora crassa has recently been reported. The N. crassa OM vesicles retained the features of the intact mitochondria concerning the dependency of insertion on the receptor protein [A. Mayer et al. (1993) J. Cell Biol. 121, 1233-1243]. In this study, OM vesicles were purified from bovine adrenal cortex mitochondria, and unilamellar proteoliposomes were reconstituted from OM vesicles using heptyl beta-thioglucoside. Both OM vesicles and the reconstituted outer membrane vesicles (ROM) were able to import porin, but unable to import the precursor of adrenodoxin, which translocates across both the outer and inner membranes of intact mitochondria. Porin insertion into both OM vesicles and ROM was inhibited in the presence of purified recombinant adrenodoxin precursor and also by ATP depletion, and was dependent on the trypsin-sensitive membrane surface factor, suggesting that the purified OM vesicles as well as ROM retained the properties of the intact OM concerning porin insertion. The protein import machinery of OM seems to be functional for the outer membrane protein without the participation of the inner membrane. The successful reconstitution of the protein import activity from solubilized OM will pave the way for further biochemical characterization of the protein import machinery of OM.
J Iwahashi; S Takaichi; K Mihara; T Omura
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  116     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1994 Jul 
Date Detail:
Created Date:  1995-01-25     Completed Date:  1995-01-25     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  156-63     Citation Subset:  IM    
Department of Molecular Biology, Graduate School of Medical Science, Kyushu University.
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MeSH Terms
Adenosine Triphosphate / physiology
Amino Acid Sequence
Biological Transport / physiology
Intracellular Membranes / metabolism*
Membrane Proteins / metabolism*
Mitochondria / metabolism*,  ultrastructure
Molecular Sequence Data
Porins / metabolism
Reg. No./Substance:
0/Liposomes; 0/Membrane Proteins; 0/Porins; 56-65-5/Adenosine Triphosphate

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