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Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes
Cells adjust to nutrient deprivation by reversible translational shutdown. This is accompanied by maintaining inactive ribosomes in a hibernation state, in which they are bound by proteins with inhibitory and protective functions. In eukaryotes, such a function was attributed to suppressor of target...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7392345/ https://www.ncbi.nlm.nih.gov/pubmed/32687489 http://dx.doi.org/10.1371/journal.pbio.3000780 |
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author | Wells, Jennifer N. Buschauer, Robert Mackens-Kiani, Timur Best, Katharina Kratzat, Hanna Berninghausen, Otto Becker, Thomas Gilbert, Wendy Cheng, Jingdong Beckmann, Roland |
author_facet | Wells, Jennifer N. Buschauer, Robert Mackens-Kiani, Timur Best, Katharina Kratzat, Hanna Berninghausen, Otto Becker, Thomas Gilbert, Wendy Cheng, Jingdong Beckmann, Roland |
author_sort | Wells, Jennifer N. |
collection | PubMed |
description | Cells adjust to nutrient deprivation by reversible translational shutdown. This is accompanied by maintaining inactive ribosomes in a hibernation state, in which they are bound by proteins with inhibitory and protective functions. In eukaryotes, such a function was attributed to suppressor of target of Myb protein 1 (Stm1; SERPINE1 mRNA-binding protein 1 [SERBP1] in mammals), and recently, late-annotated short open reading frame 2 (Lso2; coiled-coil domain containing short open reading frame 124 [CCDC124] in mammals) was found to be involved in translational recovery after starvation from stationary phase. Here, we present cryo-electron microscopy (cryo-EM) structures of translationally inactive yeast and human ribosomes. We found Lso2/CCDC124 accumulating on idle ribosomes in the nonrotated state, in contrast to Stm1/SERBP1-bound ribosomes, which display a rotated state. Lso2/CCDC124 bridges the decoding sites of the small with the GTPase activating center (GAC) of the large subunit. This position allows accommodation of the duplication of multilocus region 34 protein (Dom34)-dependent ribosome recycling system, which splits Lso2-containing, but not Stm1-containing, ribosomes. We propose a model in which Lso2 facilitates rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes. |
format | Online Article Text |
id | pubmed-7392345 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-73923452020-08-12 Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes Wells, Jennifer N. Buschauer, Robert Mackens-Kiani, Timur Best, Katharina Kratzat, Hanna Berninghausen, Otto Becker, Thomas Gilbert, Wendy Cheng, Jingdong Beckmann, Roland PLoS Biol Research Article Cells adjust to nutrient deprivation by reversible translational shutdown. This is accompanied by maintaining inactive ribosomes in a hibernation state, in which they are bound by proteins with inhibitory and protective functions. In eukaryotes, such a function was attributed to suppressor of target of Myb protein 1 (Stm1; SERPINE1 mRNA-binding protein 1 [SERBP1] in mammals), and recently, late-annotated short open reading frame 2 (Lso2; coiled-coil domain containing short open reading frame 124 [CCDC124] in mammals) was found to be involved in translational recovery after starvation from stationary phase. Here, we present cryo-electron microscopy (cryo-EM) structures of translationally inactive yeast and human ribosomes. We found Lso2/CCDC124 accumulating on idle ribosomes in the nonrotated state, in contrast to Stm1/SERBP1-bound ribosomes, which display a rotated state. Lso2/CCDC124 bridges the decoding sites of the small with the GTPase activating center (GAC) of the large subunit. This position allows accommodation of the duplication of multilocus region 34 protein (Dom34)-dependent ribosome recycling system, which splits Lso2-containing, but not Stm1-containing, ribosomes. We propose a model in which Lso2 facilitates rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes. Public Library of Science 2020-07-20 /pmc/articles/PMC7392345/ /pubmed/32687489 http://dx.doi.org/10.1371/journal.pbio.3000780 Text en © 2020 Wells et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Wells, Jennifer N. Buschauer, Robert Mackens-Kiani, Timur Best, Katharina Kratzat, Hanna Berninghausen, Otto Becker, Thomas Gilbert, Wendy Cheng, Jingdong Beckmann, Roland Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes |
title | Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes |
title_full | Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes |
title_fullStr | Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes |
title_full_unstemmed | Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes |
title_short | Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes |
title_sort | structure and function of yeast lso2 and human ccdc124 bound to hibernating ribosomes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7392345/ https://www.ncbi.nlm.nih.gov/pubmed/32687489 http://dx.doi.org/10.1371/journal.pbio.3000780 |
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