Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space Journal Article


Authors: Koll, H.; Guiard, B.; Rassow, J.; Ostermann, J.; Horwich, A. L.; Neupert, W.; Hartl, F. U.
Article Title: Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space
Abstract: Cytochrome b2 reaches the intermembrane space of mitochondria by transport into the matrix followed by export across the inner membrane. While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export. The bacterial-type export sequence in pre-cytochrome b2 functions by inhibiting the ATP-dependent release of the protein from hsp60. Release for export apparently requires, in addition to ATP, the interaction of the signal sequence with a component of the export machinery in the inner membrane. Export can occur before import is complete provided that a critical length of the polypeptide chain has been translocated into the matrix. Thus, hsp60 combines two activities: catalysis of folding of proteins destined for the matrix, and maintaining proteins in an unfolded state to facilitate their channeling between the machineries for import and export across the inner membrane. Antifolding signals such as the hydrophobic export sequence in cytochrome b2 may act as switches between these two activities. © 1992.
Keywords: nonhuman; protein conformation; proteins; protein targeting; bacteria (microorganisms); protein processing; molecular sequence data; hybrid protein; recombinant fusion proteins; saccharomyces cerevisiae; signal peptide; protein secretion; base sequence; cell fractionation; lactate dehydrogenase; catalysis; adenosine triphosphate; protein folding; mitochondrial membrane; mitochondria; biological transport; fungal proteins; heat-shock proteins; heat shock protein; protein sorting signals; chaperonins; chaperonin 60; priority journal; article; support, non-u.s. gov't; cytochrome b
Journal Title: Cell
Volume: 68
Issue: 6
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 1992-03-20
Start Page: 1163
End Page: 1175
Language: English
DOI: 10.1016/0092-8674(92)90086-r
PUBMED: 1347713
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 30 July 2019 -- Source: Scopus
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  1. F. Ulrich Hartl
    75 Hartl