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PMID: 2528694 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis.

Nature ·Vol. 341 ·No. 6238 ·1989-09-14 ·Pages 125-30

Ostermann J, Horwich AL, Neupert W, Hartl FU

Abstract

Mitochondrial heat-shock protein hsp60 functions in the folding of proteins imported into mitochondria. Folding occurs at the surface of hsp60 in an ATP-mediated reaction, followed by release of the bound polypeptides. We propose that hsp60 catalyses protein folding.

MeSH Terms
Adenosine Triphosphate/metabolism Animals Ethylmaleimide/pharmacology Heat-Shock Proteins/metabolism Humans Kinetics Mitochondria/drug effects,metabolism Neurospora/enzymology Protein Conformation Proton-Translocating ATPases/metabolism Tetrahydrofolate Dehydrogenase/metabolism
Chemicals
Heat-Shock Proteins Adenosine Triphosphate Tetrahydrofolate Dehydrogenase Proton-Translocating ATPases Ethylmaleimide
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ostermann J
Institut für Physiologische Chemie der Universität München, FRG.
Horwich A L
Neupert W
Hartl F U
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
DOI
10.1038/341125a0
Published
1989-09-14
Pages
125-30
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
PMID: 24061226
External Links
PubMed source DOI: 10.1038/341125a0 View journal details
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