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A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells
Prokaryotes can provide new genetic information to eukaryotes by horizontal gene transfer (HGT), and such transfers are likely to have been particularly consequential in the era of eukaryogenesis. Since eukaryotes are highly compartmentalized, it is worthwhile to consider the mechanisms by which new...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6219538/ https://www.ncbi.nlm.nih.gov/pubmed/30401812 http://dx.doi.org/10.1038/s41598-018-34646-7 |
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author | Lutfullahoğlu-Bal, Güleycan Seferoğlu, Ayşe Bengisu Keskin, Abdurrahman Akdoğan, Emel Dunn, Cory D. |
author_facet | Lutfullahoğlu-Bal, Güleycan Seferoğlu, Ayşe Bengisu Keskin, Abdurrahman Akdoğan, Emel Dunn, Cory D. |
author_sort | Lutfullahoğlu-Bal, Güleycan |
collection | PubMed |
description | Prokaryotes can provide new genetic information to eukaryotes by horizontal gene transfer (HGT), and such transfers are likely to have been particularly consequential in the era of eukaryogenesis. Since eukaryotes are highly compartmentalized, it is worthwhile to consider the mechanisms by which newly transferred proteins might reach diverse organellar destinations. Toward this goal, we have focused our attention upon the behavior of bacteria-derived tail anchors (TAs) expressed in the eukaryote Saccharomyces cerevisiae. In this study, we report that a predicted membrane-associated domain of the Escherichia coli YgiM protein is specifically trafficked to peroxisomes in budding yeast, can be found at a pre-peroxisomal compartment (PPC) upon disruption of peroxisomal biogenesis, and can functionally replace an endogenous, peroxisome-directed TA. Furthermore, the YgiM(TA) can localize to peroxisomes in mammalian cells. Since the YgiM(TA) plays no endogenous role in peroxisomal function or assembly, this domain is likely to serve as an excellent tool allowing further illumination of the mechanisms by which TAs can travel to peroxisomes. Moreover, our findings emphasize the ease with which bacteria-derived sequences might target to organelles in eukaryotic cells following HGT, and we discuss the importance of flexible recognition of organelle targeting information during and after eukaryogenesis. |
format | Online Article Text |
id | pubmed-6219538 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-62195382018-11-07 A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells Lutfullahoğlu-Bal, Güleycan Seferoğlu, Ayşe Bengisu Keskin, Abdurrahman Akdoğan, Emel Dunn, Cory D. Sci Rep Article Prokaryotes can provide new genetic information to eukaryotes by horizontal gene transfer (HGT), and such transfers are likely to have been particularly consequential in the era of eukaryogenesis. Since eukaryotes are highly compartmentalized, it is worthwhile to consider the mechanisms by which newly transferred proteins might reach diverse organellar destinations. Toward this goal, we have focused our attention upon the behavior of bacteria-derived tail anchors (TAs) expressed in the eukaryote Saccharomyces cerevisiae. In this study, we report that a predicted membrane-associated domain of the Escherichia coli YgiM protein is specifically trafficked to peroxisomes in budding yeast, can be found at a pre-peroxisomal compartment (PPC) upon disruption of peroxisomal biogenesis, and can functionally replace an endogenous, peroxisome-directed TA. Furthermore, the YgiM(TA) can localize to peroxisomes in mammalian cells. Since the YgiM(TA) plays no endogenous role in peroxisomal function or assembly, this domain is likely to serve as an excellent tool allowing further illumination of the mechanisms by which TAs can travel to peroxisomes. Moreover, our findings emphasize the ease with which bacteria-derived sequences might target to organelles in eukaryotic cells following HGT, and we discuss the importance of flexible recognition of organelle targeting information during and after eukaryogenesis. Nature Publishing Group UK 2018-11-06 /pmc/articles/PMC6219538/ /pubmed/30401812 http://dx.doi.org/10.1038/s41598-018-34646-7 Text en © The Author(s) 2018 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 Lutfullahoğlu-Bal, Güleycan Seferoğlu, Ayşe Bengisu Keskin, Abdurrahman Akdoğan, Emel Dunn, Cory D. A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells |
title | A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells |
title_full | A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells |
title_fullStr | A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells |
title_full_unstemmed | A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells |
title_short | A bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells |
title_sort | bacteria-derived tail anchor localizes to peroxisomes in yeast and mammalian cells |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6219538/ https://www.ncbi.nlm.nih.gov/pubmed/30401812 http://dx.doi.org/10.1038/s41598-018-34646-7 |
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