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Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast
During eukaryotic ribosome biogenesis, pre-ribosomes travel from the nucleolus, where assembly is initiated, to the nucleoplasm and then are exported to the cytoplasm, where assembly concludes. Although nuclear export of pre-ribosomes has been extensively investigated, the release of pre-ribosomes f...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10639060/ https://www.ncbi.nlm.nih.gov/pubmed/35736211 http://dx.doi.org/10.1093/nar/gkac430 |
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author | LaPeruta, Amber J Micic, Jelena Woolford Jr., John L |
author_facet | LaPeruta, Amber J Micic, Jelena Woolford Jr., John L |
author_sort | LaPeruta, Amber J |
collection | PubMed |
description | During eukaryotic ribosome biogenesis, pre-ribosomes travel from the nucleolus, where assembly is initiated, to the nucleoplasm and then are exported to the cytoplasm, where assembly concludes. Although nuclear export of pre-ribosomes has been extensively investigated, the release of pre-ribosomes from the nucleolus is an understudied phenomenon. Initial data indicate that unfolded rRNA interacts in trans with nucleolar components and that, when rRNA folds due to ribosomal protein (RP) binding, the number of trans interactions drops below the threshold necessary for nucleolar retention. To validate and expand on this idea, we performed a bioinformatic analysis of the protein components of the Saccharomyces cerevisiae ribosome assembly pathway. We found that ribosome biogenesis factors (RiBi factors) contain significantly more predicted trans interacting regions than RPs. We also analyzed cryo-EM structures of ribosome assembly intermediates to determine how nucleolar pre-ribosomes differ from post-nucleolar pre-ribosomes, specifically the capacity of RPs, RiBi factors, and rRNA components to interact in trans. We observed a significant decrease in the theoretical trans-interacting capability of pre-ribosomes between nucleolar and post-nucleolar stages of assembly due to the release of RiBi factors from particles and the folding of rRNA. Here, we provide a mechanism for the release of pre-ribosomes from the nucleolus. |
format | Online Article Text |
id | pubmed-10639060 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-106390602023-11-15 Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast LaPeruta, Amber J Micic, Jelena Woolford Jr., John L Nucleic Acids Res Computational Biology During eukaryotic ribosome biogenesis, pre-ribosomes travel from the nucleolus, where assembly is initiated, to the nucleoplasm and then are exported to the cytoplasm, where assembly concludes. Although nuclear export of pre-ribosomes has been extensively investigated, the release of pre-ribosomes from the nucleolus is an understudied phenomenon. Initial data indicate that unfolded rRNA interacts in trans with nucleolar components and that, when rRNA folds due to ribosomal protein (RP) binding, the number of trans interactions drops below the threshold necessary for nucleolar retention. To validate and expand on this idea, we performed a bioinformatic analysis of the protein components of the Saccharomyces cerevisiae ribosome assembly pathway. We found that ribosome biogenesis factors (RiBi factors) contain significantly more predicted trans interacting regions than RPs. We also analyzed cryo-EM structures of ribosome assembly intermediates to determine how nucleolar pre-ribosomes differ from post-nucleolar pre-ribosomes, specifically the capacity of RPs, RiBi factors, and rRNA components to interact in trans. We observed a significant decrease in the theoretical trans-interacting capability of pre-ribosomes between nucleolar and post-nucleolar stages of assembly due to the release of RiBi factors from particles and the folding of rRNA. Here, we provide a mechanism for the release of pre-ribosomes from the nucleolus. Oxford University Press 2022-06-23 /pmc/articles/PMC10639060/ /pubmed/35736211 http://dx.doi.org/10.1093/nar/gkac430 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Computational Biology LaPeruta, Amber J Micic, Jelena Woolford Jr., John L Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast |
title | Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast |
title_full | Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast |
title_fullStr | Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast |
title_full_unstemmed | Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast |
title_short | Additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast |
title_sort | additional principles that govern the release of pre-ribosomes from the nucleolus into the nucleoplasm in yeast |
topic | Computational Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10639060/ https://www.ncbi.nlm.nih.gov/pubmed/35736211 http://dx.doi.org/10.1093/nar/gkac430 |
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