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How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?

A multisubunit translocase of the outer mitochondrial membrane (TOM complex) mediates both the import of mitochondrial precursor proteins into the internal compartments of the organelle and the insertion of proteins residing in the mitochondrial outer membrane. The proposed β-barrel structure of Tom...

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Detalles Bibliográficos
Autor principal: Rapaport, Doron
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171261/
https://www.ncbi.nlm.nih.gov/pubmed/16260501
http://dx.doi.org/10.1083/jcb.200507147
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author Rapaport, Doron
author_facet Rapaport, Doron
author_sort Rapaport, Doron
collection PubMed
description A multisubunit translocase of the outer mitochondrial membrane (TOM complex) mediates both the import of mitochondrial precursor proteins into the internal compartments of the organelle and the insertion of proteins residing in the mitochondrial outer membrane. The proposed β-barrel structure of Tom40, the pore-forming component of the translocase, raises the question of how the apparent uninterrupted β-barrel topology can be compatible with a role of Tom40 in releasing membrane proteins into the lipid core of the bilayer. In this review, I discuss insertion mechanisms of proteins into the outer membrane and present alternative models based on the opening of a multisubunit β-barrel TOM structure or on the interaction of outer membrane precursors with the outer face of the Tom40 β-barrel structure.
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spelling pubmed-21712612008-03-05 How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane? Rapaport, Doron J Cell Biol Reviews A multisubunit translocase of the outer mitochondrial membrane (TOM complex) mediates both the import of mitochondrial precursor proteins into the internal compartments of the organelle and the insertion of proteins residing in the mitochondrial outer membrane. The proposed β-barrel structure of Tom40, the pore-forming component of the translocase, raises the question of how the apparent uninterrupted β-barrel topology can be compatible with a role of Tom40 in releasing membrane proteins into the lipid core of the bilayer. In this review, I discuss insertion mechanisms of proteins into the outer membrane and present alternative models based on the opening of a multisubunit β-barrel TOM structure or on the interaction of outer membrane precursors with the outer face of the Tom40 β-barrel structure. The Rockefeller University Press 2005-11-07 /pmc/articles/PMC2171261/ /pubmed/16260501 http://dx.doi.org/10.1083/jcb.200507147 Text en Copyright © 2005, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Reviews
Rapaport, Doron
How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
title How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
title_full How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
title_fullStr How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
title_full_unstemmed How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
title_short How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
title_sort how does the tom complex mediate insertion of precursor proteins into the mitochondrial outer membrane?
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171261/
https://www.ncbi.nlm.nih.gov/pubmed/16260501
http://dx.doi.org/10.1083/jcb.200507147
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