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CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state
Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be shut down almost entirely by inhibiting ribosomal function. Here we investigated eukaryotic hibernat...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10522483/ https://www.ncbi.nlm.nih.gov/pubmed/37709902 http://dx.doi.org/10.1038/s41564-023-01469-w |
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author | McLaren, Mathew Conners, Rebecca Isupov, Michail N. Gil-Díez, Patricia Gambelli, Lavinia Gold, Vicki A. M. Walter, Andreas Connell, Sean R. Williams, Bryony Daum, Bertram |
author_facet | McLaren, Mathew Conners, Rebecca Isupov, Michail N. Gil-Díez, Patricia Gambelli, Lavinia Gold, Vicki A. M. Walter, Andreas Connell, Sean R. Williams, Bryony Daum, Bertram |
author_sort | McLaren, Mathew |
collection | PubMed |
description | Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be shut down almost entirely by inhibiting ribosomal function. Here we investigated eukaryotic hibernating ribosomes from the microsporidian parasite Spraguea lophii in situ by a combination of electron cryo-tomography and single-particle electron cryo-microscopy. We show that microsporidian spores contain hibernating ribosomes that are locked in a dimeric (100S) state, which is formed by a unique dimerization mechanism involving the beak region. The ribosomes within the dimer are fully assembled, suggesting that they are ready to be activated once the host cell is invaded. This study provides structural evidence for dimerization acting as a mechanism for ribosomal hibernation in microsporidia, and therefore demonstrates that eukaryotes utilize this mechanism in translational control. |
format | Online Article Text |
id | pubmed-10522483 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-105224832023-09-28 CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state McLaren, Mathew Conners, Rebecca Isupov, Michail N. Gil-Díez, Patricia Gambelli, Lavinia Gold, Vicki A. M. Walter, Andreas Connell, Sean R. Williams, Bryony Daum, Bertram Nat Microbiol Article Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be shut down almost entirely by inhibiting ribosomal function. Here we investigated eukaryotic hibernating ribosomes from the microsporidian parasite Spraguea lophii in situ by a combination of electron cryo-tomography and single-particle electron cryo-microscopy. We show that microsporidian spores contain hibernating ribosomes that are locked in a dimeric (100S) state, which is formed by a unique dimerization mechanism involving the beak region. The ribosomes within the dimer are fully assembled, suggesting that they are ready to be activated once the host cell is invaded. This study provides structural evidence for dimerization acting as a mechanism for ribosomal hibernation in microsporidia, and therefore demonstrates that eukaryotes utilize this mechanism in translational control. Nature Publishing Group UK 2023-09-14 2023 /pmc/articles/PMC10522483/ /pubmed/37709902 http://dx.doi.org/10.1038/s41564-023-01469-w Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article McLaren, Mathew Conners, Rebecca Isupov, Michail N. Gil-Díez, Patricia Gambelli, Lavinia Gold, Vicki A. M. Walter, Andreas Connell, Sean R. Williams, Bryony Daum, Bertram CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state |
title | CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state |
title_full | CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state |
title_fullStr | CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state |
title_full_unstemmed | CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state |
title_short | CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state |
title_sort | cryoem reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10522483/ https://www.ncbi.nlm.nih.gov/pubmed/37709902 http://dx.doi.org/10.1038/s41564-023-01469-w |
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