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The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins

The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of β-barrel proteins of the...

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Autores principales: Becker, Thomas, Wenz, Lena-Sophie, Krüger, Vivien, Lehmann, Waltraut, Müller, Judith M., Goroncy, Luise, Zufall, Nicole, Lithgow, Trevor, Guiard, Bernard, Chacinska, Agnieszka, Wagner, Richard, Meisinger, Chris, Pfanner, Nikolaus
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153637/
https://www.ncbi.nlm.nih.gov/pubmed/21825073
http://dx.doi.org/10.1083/jcb.201102044
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author Becker, Thomas
Wenz, Lena-Sophie
Krüger, Vivien
Lehmann, Waltraut
Müller, Judith M.
Goroncy, Luise
Zufall, Nicole
Lithgow, Trevor
Guiard, Bernard
Chacinska, Agnieszka
Wagner, Richard
Meisinger, Chris
Pfanner, Nikolaus
author_facet Becker, Thomas
Wenz, Lena-Sophie
Krüger, Vivien
Lehmann, Waltraut
Müller, Judith M.
Goroncy, Luise
Zufall, Nicole
Lithgow, Trevor
Guiard, Bernard
Chacinska, Agnieszka
Wagner, Richard
Meisinger, Chris
Pfanner, Nikolaus
author_sort Becker, Thomas
collection PubMed
description The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of β-barrel proteins of the outer membrane. Several α-helical outer membrane proteins are known to carry multiple transmembrane segments; however, only limited information is available on the biogenesis of these proteins. We report that mitochondria lacking the mitochondrial import protein 1 (Mim1) are impaired in the biogenesis of multispanning outer membrane proteins, whereas overexpression of Mim1 stimulates their import. The Mim1 complex cooperates with the receptor Tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. We conclude that the Mim1 complex plays a central role in the import of α-helical outer membrane proteins with multiple transmembrane segments.
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spelling pubmed-31536372012-02-08 The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins Becker, Thomas Wenz, Lena-Sophie Krüger, Vivien Lehmann, Waltraut Müller, Judith M. Goroncy, Luise Zufall, Nicole Lithgow, Trevor Guiard, Bernard Chacinska, Agnieszka Wagner, Richard Meisinger, Chris Pfanner, Nikolaus J Cell Biol Research Articles The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of β-barrel proteins of the outer membrane. Several α-helical outer membrane proteins are known to carry multiple transmembrane segments; however, only limited information is available on the biogenesis of these proteins. We report that mitochondria lacking the mitochondrial import protein 1 (Mim1) are impaired in the biogenesis of multispanning outer membrane proteins, whereas overexpression of Mim1 stimulates their import. The Mim1 complex cooperates with the receptor Tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. We conclude that the Mim1 complex plays a central role in the import of α-helical outer membrane proteins with multiple transmembrane segments. The Rockefeller University Press 2011-08-08 /pmc/articles/PMC3153637/ /pubmed/21825073 http://dx.doi.org/10.1083/jcb.201102044 Text en © 2011 Becker et al. 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 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Becker, Thomas
Wenz, Lena-Sophie
Krüger, Vivien
Lehmann, Waltraut
Müller, Judith M.
Goroncy, Luise
Zufall, Nicole
Lithgow, Trevor
Guiard, Bernard
Chacinska, Agnieszka
Wagner, Richard
Meisinger, Chris
Pfanner, Nikolaus
The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins
title The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins
title_full The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins
title_fullStr The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins
title_full_unstemmed The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins
title_short The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins
title_sort mitochondrial import protein mim1 promotes biogenesis of multispanning outer membrane proteins
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153637/
https://www.ncbi.nlm.nih.gov/pubmed/21825073
http://dx.doi.org/10.1083/jcb.201102044
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