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Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus
The nucleolus is a non-membrane bound organelle central to ribosome biogenesis. The nucleolus contains a mix of proteins and RNA and has 3 known nucleolar compartments: the fibrillar center (FC), the dense fibrillar component (DFC), and the granular component (GC). The spatial organization of the nu...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10662738/ https://www.ncbi.nlm.nih.gov/pubmed/37943867 http://dx.doi.org/10.1371/journal.pbio.3002378 |
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author | Lavering, Emily D. Gandhamaneni, Maunika Weeks, Daniel L. |
author_facet | Lavering, Emily D. Gandhamaneni, Maunika Weeks, Daniel L. |
author_sort | Lavering, Emily D. |
collection | PubMed |
description | The nucleolus is a non-membrane bound organelle central to ribosome biogenesis. The nucleolus contains a mix of proteins and RNA and has 3 known nucleolar compartments: the fibrillar center (FC), the dense fibrillar component (DFC), and the granular component (GC). The spatial organization of the nucleolus is influenced by the phase separation properties of nucleolar proteins, the presence of RNA, protein modification, and cellular activity. Many nucleolar proteins appear to concentrate within the borders of the compartments. We investigated whether the intrinsically disordered regions from several proteins provided the information needed to establish specific compartment localization using Xenopus laevis oocytes. For the proteins we tested, the disordered regions were not sufficient to direct specific domain localization and appear dispensable with respect to compartmentalization. Among the proteins that colocalize to the DFC are the quartet that comprise the box H/ACA pseudouridylation complex. In contrast to the insufficiency of IDRs to direct compartment localization, we found that the DFC accumulation of 2 box H/ACA proteins, Gar1 and Nhp2, was disrupted by mutations that were previously shown to reduce their ability to join the box H/ACA complex. Using a nanobody to introduce novel binding to a different DFC localized protein, we restored the localization of the mutated forms of Gar1 and Nhp2. |
format | Online Article Text |
id | pubmed-10662738 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-106627382023-11-09 Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus Lavering, Emily D. Gandhamaneni, Maunika Weeks, Daniel L. PLoS Biol Short Reports The nucleolus is a non-membrane bound organelle central to ribosome biogenesis. The nucleolus contains a mix of proteins and RNA and has 3 known nucleolar compartments: the fibrillar center (FC), the dense fibrillar component (DFC), and the granular component (GC). The spatial organization of the nucleolus is influenced by the phase separation properties of nucleolar proteins, the presence of RNA, protein modification, and cellular activity. Many nucleolar proteins appear to concentrate within the borders of the compartments. We investigated whether the intrinsically disordered regions from several proteins provided the information needed to establish specific compartment localization using Xenopus laevis oocytes. For the proteins we tested, the disordered regions were not sufficient to direct specific domain localization and appear dispensable with respect to compartmentalization. Among the proteins that colocalize to the DFC are the quartet that comprise the box H/ACA pseudouridylation complex. In contrast to the insufficiency of IDRs to direct compartment localization, we found that the DFC accumulation of 2 box H/ACA proteins, Gar1 and Nhp2, was disrupted by mutations that were previously shown to reduce their ability to join the box H/ACA complex. Using a nanobody to introduce novel binding to a different DFC localized protein, we restored the localization of the mutated forms of Gar1 and Nhp2. Public Library of Science 2023-11-09 /pmc/articles/PMC10662738/ /pubmed/37943867 http://dx.doi.org/10.1371/journal.pbio.3002378 Text en © 2023 Lavering et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://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 | Short Reports Lavering, Emily D. Gandhamaneni, Maunika Weeks, Daniel L. Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus |
title | Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus |
title_full | Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus |
title_fullStr | Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus |
title_full_unstemmed | Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus |
title_short | Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus |
title_sort | intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus |
topic | Short Reports |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10662738/ https://www.ncbi.nlm.nih.gov/pubmed/37943867 http://dx.doi.org/10.1371/journal.pbio.3002378 |
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