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Myristoyl group-aided protein import into the mitochondrial intermembrane space
The MICOS complex mediates formation of the crista junctions in mitochondria. Here we analyzed the mitochondrial import pathways for the six yeast MICOS subunits as a step toward understanding of the assembly mechanisms of the MICOS complex. Mic10, Mic12, Mic26, Mic27, and Mic60 used the presequence...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6362269/ https://www.ncbi.nlm.nih.gov/pubmed/30718713 http://dx.doi.org/10.1038/s41598-018-38016-1 |
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author | Ueda, Eri Tamura, Yasushi Sakaue, Haruka Kawano, Shin Kakuta, Chika Matsumoto, Shunsuke Endo, Toshiya |
author_facet | Ueda, Eri Tamura, Yasushi Sakaue, Haruka Kawano, Shin Kakuta, Chika Matsumoto, Shunsuke Endo, Toshiya |
author_sort | Ueda, Eri |
collection | PubMed |
description | The MICOS complex mediates formation of the crista junctions in mitochondria. Here we analyzed the mitochondrial import pathways for the six yeast MICOS subunits as a step toward understanding of the assembly mechanisms of the MICOS complex. Mic10, Mic12, Mic26, Mic27, and Mic60 used the presequence pathway to reach the intermembrane space (IMS). In contrast, Mic19 took the TIM40/MIA pathway, through its CHCH domain, to reach the IMS. Unlike canonical TIM40/MIA substrates, presence of the N-terminal unfolded DUF domain impaired the import efficiency of Mic19, yet N-terminal myristoylation of Mic19 circumvented this effect. The myristoyl group of Mic19 binds to Tom20 of the TOM complex as well as the outer membrane, which may lead to “entropy pushing” of the DUF domain followed by the CHCH domain of Mic19 into the import channel, thereby achieving efficient import. |
format | Online Article Text |
id | pubmed-6362269 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-63622692019-02-07 Myristoyl group-aided protein import into the mitochondrial intermembrane space Ueda, Eri Tamura, Yasushi Sakaue, Haruka Kawano, Shin Kakuta, Chika Matsumoto, Shunsuke Endo, Toshiya Sci Rep Article The MICOS complex mediates formation of the crista junctions in mitochondria. Here we analyzed the mitochondrial import pathways for the six yeast MICOS subunits as a step toward understanding of the assembly mechanisms of the MICOS complex. Mic10, Mic12, Mic26, Mic27, and Mic60 used the presequence pathway to reach the intermembrane space (IMS). In contrast, Mic19 took the TIM40/MIA pathway, through its CHCH domain, to reach the IMS. Unlike canonical TIM40/MIA substrates, presence of the N-terminal unfolded DUF domain impaired the import efficiency of Mic19, yet N-terminal myristoylation of Mic19 circumvented this effect. The myristoyl group of Mic19 binds to Tom20 of the TOM complex as well as the outer membrane, which may lead to “entropy pushing” of the DUF domain followed by the CHCH domain of Mic19 into the import channel, thereby achieving efficient import. Nature Publishing Group UK 2019-02-04 /pmc/articles/PMC6362269/ /pubmed/30718713 http://dx.doi.org/10.1038/s41598-018-38016-1 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Ueda, Eri Tamura, Yasushi Sakaue, Haruka Kawano, Shin Kakuta, Chika Matsumoto, Shunsuke Endo, Toshiya Myristoyl group-aided protein import into the mitochondrial intermembrane space |
title | Myristoyl group-aided protein import into the mitochondrial intermembrane space |
title_full | Myristoyl group-aided protein import into the mitochondrial intermembrane space |
title_fullStr | Myristoyl group-aided protein import into the mitochondrial intermembrane space |
title_full_unstemmed | Myristoyl group-aided protein import into the mitochondrial intermembrane space |
title_short | Myristoyl group-aided protein import into the mitochondrial intermembrane space |
title_sort | myristoyl group-aided protein import into the mitochondrial intermembrane space |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6362269/ https://www.ncbi.nlm.nih.gov/pubmed/30718713 http://dx.doi.org/10.1038/s41598-018-38016-1 |
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