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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...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2011
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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. |
format | Online Article Text |
id | pubmed-3153637 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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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