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Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives
BACKGROUND: An ancestral trait of eukaryotic cells is the presence of mitochondria as an essential element for function and survival. Proper functioning of mitochondria depends on the import of nearly all proteins that is performed by complexes located in both mitochondrial membranes. The complexes...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4744386/ https://www.ncbi.nlm.nih.gov/pubmed/26852331 http://dx.doi.org/10.1186/s12864-016-2402-2 |
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author | Buczek, Dorota Wojtkowska, Małgorzata Suzuki, Yutaka Sonobe, Seiji Nishigami, Yukinori Antoniewicz, Monika Kmita, Hanna Makałowski, Wojciech |
author_facet | Buczek, Dorota Wojtkowska, Małgorzata Suzuki, Yutaka Sonobe, Seiji Nishigami, Yukinori Antoniewicz, Monika Kmita, Hanna Makałowski, Wojciech |
author_sort | Buczek, Dorota |
collection | PubMed |
description | BACKGROUND: An ancestral trait of eukaryotic cells is the presence of mitochondria as an essential element for function and survival. Proper functioning of mitochondria depends on the import of nearly all proteins that is performed by complexes located in both mitochondrial membranes. The complexes have been proposed to contain subunits formed by proteins common to all eukaryotes and additional subunits regarded as lineage specific. Since Amoebozoa is poorly sampled for the complexes we investigated the outer membrane complexes, namely TOM, TOB/SAM and ERMES complexes, using available genome and transcriptome sequences, including transcriptomes assembled by us. RESULTS: The results indicate differences in the organization of the Amoebozoa TOM, TOB/SAM and ERMES complexes, with the TOM complex appearing to be the most diverse. This is reflected by differences in the number of involved subunits and in similarities to the cognate proteins of representatives from different supergroups of eukaryotes. CONCLUSIONS: The obtained results clearly demonstrate structural variability/diversity of these complexes in the Amoebozoa lineage and the reduction of their complexity as compared with the same complexes of model organisms. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12864-016-2402-2) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4744386 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-47443862016-02-07 Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives Buczek, Dorota Wojtkowska, Małgorzata Suzuki, Yutaka Sonobe, Seiji Nishigami, Yukinori Antoniewicz, Monika Kmita, Hanna Makałowski, Wojciech BMC Genomics Research Article BACKGROUND: An ancestral trait of eukaryotic cells is the presence of mitochondria as an essential element for function and survival. Proper functioning of mitochondria depends on the import of nearly all proteins that is performed by complexes located in both mitochondrial membranes. The complexes have been proposed to contain subunits formed by proteins common to all eukaryotes and additional subunits regarded as lineage specific. Since Amoebozoa is poorly sampled for the complexes we investigated the outer membrane complexes, namely TOM, TOB/SAM and ERMES complexes, using available genome and transcriptome sequences, including transcriptomes assembled by us. RESULTS: The results indicate differences in the organization of the Amoebozoa TOM, TOB/SAM and ERMES complexes, with the TOM complex appearing to be the most diverse. This is reflected by differences in the number of involved subunits and in similarities to the cognate proteins of representatives from different supergroups of eukaryotes. CONCLUSIONS: The obtained results clearly demonstrate structural variability/diversity of these complexes in the Amoebozoa lineage and the reduction of their complexity as compared with the same complexes of model organisms. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12864-016-2402-2) contains supplementary material, which is available to authorized users. BioMed Central 2016-02-06 /pmc/articles/PMC4744386/ /pubmed/26852331 http://dx.doi.org/10.1186/s12864-016-2402-2 Text en © Buczek et al. 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Buczek, Dorota Wojtkowska, Małgorzata Suzuki, Yutaka Sonobe, Seiji Nishigami, Yukinori Antoniewicz, Monika Kmita, Hanna Makałowski, Wojciech Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives |
title | Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives |
title_full | Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives |
title_fullStr | Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives |
title_full_unstemmed | Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives |
title_short | Protein import complexes in the mitochondrial outer membrane of Amoebozoa representatives |
title_sort | protein import complexes in the mitochondrial outer membrane of amoebozoa representatives |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4744386/ https://www.ncbi.nlm.nih.gov/pubmed/26852331 http://dx.doi.org/10.1186/s12864-016-2402-2 |
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