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PMID: 2841112 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Unfolding and refolding of a purified precursor protein during import into isolated mitochondria.

The EMBO journal ·Vol. 7 ·No. 4 ·1988-04-00 ·Pages 1139-45

Eilers M, Hwang S, Schatz G

Abstract

A purified mitochondrial precursor protein unfolds to a protease-sensitive conformation at the surface of isolated mitochondria before being imported into the organelles. This unfolding is stimulated by a potential across the mitochondrial inner membrane, but does not require ATP. In contrast, import of the surface-bound unfolded precursor requires ATP, but no potential; it is accompanied by a refolding inside the mitochondria.

MeSH Terms
Animals Electron Transport Complex IV/genetics,metabolism Enzyme Precursors/genetics Macromolecular Substances Mice Mitochondria/enzymology Protein Conformation Protein Denaturation Recombinant Fusion Proteins/metabolism Recombinant Proteins/metabolism Saccharomyces cerevisiae/enzymology,genetics Tetrahydrofolate Dehydrogenase/genetics,metabolism Urea/pharmacology
Chemicals
Enzyme Precursors Macromolecular Substances Recombinant Fusion Proteins Recombinant Proteins Urea Tetrahydrofolate Dehydrogenase Electron Transport Complex IV
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Eilers M
University of Basel, Department of Biochemistry, Switzerland.
Hwang S
Schatz G
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24 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1988-04-00
Pages
1139-45
Language
English
Region
England
NLM ID
8208664
PMCID
PMC454448
Subset
IM
Grants
NIGMS NIH HHS · CBY-1 1 R01 GM37803-01 · United States
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