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The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals
The TOM40 complex is a protein translocator in the mitochondrial outer membrane and consists of several different subunits. Among them, Tom40 is a central subunit that constitutes a protein-conducting channel by forming a β-barrel structure. To probe the nature of the assembly process of Tom40 in th...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3469510/ https://www.ncbi.nlm.nih.gov/pubmed/22933571 http://dx.doi.org/10.1091/mbc.E12-03-0202 |
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author | Shiota, Takuya Maruyama, Miyuki Miura, Mami Tamura, Yasushi Yamano, Koji Esaki, Masatoshi Endo, Toshiya |
author_facet | Shiota, Takuya Maruyama, Miyuki Miura, Mami Tamura, Yasushi Yamano, Koji Esaki, Masatoshi Endo, Toshiya |
author_sort | Shiota, Takuya |
collection | PubMed |
description | The TOM40 complex is a protein translocator in the mitochondrial outer membrane and consists of several different subunits. Among them, Tom40 is a central subunit that constitutes a protein-conducting channel by forming a β-barrel structure. To probe the nature of the assembly process of Tom40 in the outer membrane, we attached various mitochondrial presequences to Tom40 that possess sorting information for the intermembrane space (IMS), inner membrane, and matrix and would compete with the inherent Tom40 assembly process. We analyzed the mitochondrial import of those fusion proteins in vitro. Tom40 crossed the outer membrane and/or inner membrane even in the presence of various sorting signals. N-terminal anchorage of the attached presequence to the inner membrane did not prevent Tom40 from associating with the TOB/SAM complex, although it impaired its efficient release from the TOB complex in vitro but not in vivo. The IMS or matrix-targeting presequence attached to Tom40 was effective in substituting for the requirement for small Tim proteins in the IMS for the translocation of Tom40 across the outer membrane. These results provide insight into the mechanism responsible for the precise delivery of β-barrel proteins to the outer mitochondrial membrane. |
format | Online Article Text |
id | pubmed-3469510 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-34695102012-12-30 The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals Shiota, Takuya Maruyama, Miyuki Miura, Mami Tamura, Yasushi Yamano, Koji Esaki, Masatoshi Endo, Toshiya Mol Biol Cell Articles The TOM40 complex is a protein translocator in the mitochondrial outer membrane and consists of several different subunits. Among them, Tom40 is a central subunit that constitutes a protein-conducting channel by forming a β-barrel structure. To probe the nature of the assembly process of Tom40 in the outer membrane, we attached various mitochondrial presequences to Tom40 that possess sorting information for the intermembrane space (IMS), inner membrane, and matrix and would compete with the inherent Tom40 assembly process. We analyzed the mitochondrial import of those fusion proteins in vitro. Tom40 crossed the outer membrane and/or inner membrane even in the presence of various sorting signals. N-terminal anchorage of the attached presequence to the inner membrane did not prevent Tom40 from associating with the TOB/SAM complex, although it impaired its efficient release from the TOB complex in vitro but not in vivo. The IMS or matrix-targeting presequence attached to Tom40 was effective in substituting for the requirement for small Tim proteins in the IMS for the translocation of Tom40 across the outer membrane. These results provide insight into the mechanism responsible for the precise delivery of β-barrel proteins to the outer mitochondrial membrane. The American Society for Cell Biology 2012-10-15 /pmc/articles/PMC3469510/ /pubmed/22933571 http://dx.doi.org/10.1091/mbc.E12-03-0202 Text en © 2012 Shiota et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Shiota, Takuya Maruyama, Miyuki Miura, Mami Tamura, Yasushi Yamano, Koji Esaki, Masatoshi Endo, Toshiya The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals |
title | The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals |
title_full | The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals |
title_fullStr | The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals |
title_full_unstemmed | The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals |
title_short | The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals |
title_sort | tom40 assembly process probed using the attachment of different intramitochondrial sorting signals |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3469510/ https://www.ncbi.nlm.nih.gov/pubmed/22933571 http://dx.doi.org/10.1091/mbc.E12-03-0202 |
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