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

J Ostermann; A L Horwich; W Neupert; F U Hartl

doi:10.1038/341125a0

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

Nature. 1989 Sep 14;341(6238):125-30. doi: 10.1038/341125a0.

Authors

J Ostermann¹, A L Horwich, W Neupert, F U Hartl

Affiliation

¹ Institut für Physiologische Chemie der Universität München, FRG.

PMID: 2528694
DOI: 10.1038/341125a0

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Adenosine Triphosphate / metabolism*
Animals
Ethylmaleimide / pharmacology
Heat-Shock Proteins / metabolism*
Humans
Kinetics
Mitochondria / drug effects
Mitochondria / metabolism*
Neurospora / enzymology
Protein Conformation*
Proton-Translocating ATPases / metabolism*
Tetrahydrofolate Dehydrogenase / metabolism*

Substances

Heat-Shock Proteins
Adenosine Triphosphate
Tetrahydrofolate Dehydrogenase
Proton-Translocating ATPases
Ethylmaleimide