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Neupert W, Pfanner N. Roles of molecular chaperones in protein targeting to mitochondria. Philos Trans R Soc Lond B Biol Sci. 1993;339(1289):355-61; discussion 361-2doi: 10.1098/rstb.1993.0034.
Neupert, W., & Pfanner, N. (1993). Roles of molecular chaperones in protein targeting to mitochondria. Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 339(1289), 355-61; discussion 361-2. https://doi.org/10.1098/rstb.1993.0034
Neupert, W, and Pfanner, N. "Roles of molecular chaperones in protein targeting to mitochondria." Philosophical transactions of the Royal Society of London. Series B, Biological sciences vol. 339,1289 (1993): 355-61; discussion 361-2. doi: https://doi.org/10.1098/rstb.1993.0034
Neupert W, Pfanner N. Roles of molecular chaperones in protein targeting to mitochondria. Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29;339(1289):355-61; discussion 361-2. doi: 10.1098/rstb.1993.0034. PMID: 8098540.
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Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29;339(1289):355-61; discussion 361-2. doi: 10.1098/rstb.1993.0034.

Roles of molecular chaperones in protein targeting to mitochondria.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences

W Neupert, N Pfanner

Affiliations

  1. Institut für Physiologische Chemie der Universität München, F.R.G.

PMID: 8098540 DOI: 10.1098/rstb.1993.0034

Abstract

Molecular chaperones are essential components of the machinery facilitating import of nuclear-encoded proteins into the mitochondria. They act at several steps of the complex import pathway. Cytosolic hsp 70 appears to contribute to maintaining precursors in a translocation-competent conformation. Mitochondrial hsp 70 has a distinct role in driving translocation across outer and inner mitochondrial membranes and probably in supporting unfolding of precursors in the cytosol. Hsp 60 in the matrix is involved in facilitating folding and assembly of imported polypeptide chains.

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