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A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains
Despite having high-resolution structures for eukaryotic large ribosomal subunits, it remained unclear how these ribonucleoprotein complexes are constructed in living cells. Nevertheless, knowing where ribosomal proteins interact with ribosomal RNA (rRNA) provides a strategic platform to investigate...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909792/ https://www.ncbi.nlm.nih.gov/pubmed/24449272 http://dx.doi.org/10.1101/gad.228825.113 |
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author | Gamalinda, Michael Ohmayer, Uli Jakovljevic, Jelena Kumcuoglu, Beril Woolford, Joshua Mbom, Bertrade Lin, Lawrence Woolford, John L. |
author_facet | Gamalinda, Michael Ohmayer, Uli Jakovljevic, Jelena Kumcuoglu, Beril Woolford, Joshua Mbom, Bertrade Lin, Lawrence Woolford, John L. |
author_sort | Gamalinda, Michael |
collection | PubMed |
description | Despite having high-resolution structures for eukaryotic large ribosomal subunits, it remained unclear how these ribonucleoprotein complexes are constructed in living cells. Nevertheless, knowing where ribosomal proteins interact with ribosomal RNA (rRNA) provides a strategic platform to investigate the connection between spatial and temporal aspects of 60S subunit biogenesis. We previously found that the function of individual yeast large subunit ribosomal proteins (RPLs) in precursor rRNA (pre-rRNA) processing correlates with their location in the structure of mature 60S subunits. This observation suggested that there is an order by which 60S subunits are formed. To test this model, we used proteomic approaches to assay changes in the levels of ribosomal proteins and assembly factors in preribosomes when RPLs functioning in early, middle, and late steps of pre-60S assembly are depleted. Our results demonstrate that structural domains of eukaryotic 60S ribosomal subunits are formed in a hierarchical fashion. Assembly begins at the convex solvent side, followed by the polypeptide exit tunnel, the intersubunit side, and finally the central protuberance. This model provides an initial paradigm for the sequential assembly of eukaryotic 60S subunits. Our results reveal striking differences and similarities between assembly of bacterial and eukaryotic large ribosomal subunits, providing insights into how these RNA–protein particles evolved. |
format | Online Article Text |
id | pubmed-3909792 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-39097922014-07-15 A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains Gamalinda, Michael Ohmayer, Uli Jakovljevic, Jelena Kumcuoglu, Beril Woolford, Joshua Mbom, Bertrade Lin, Lawrence Woolford, John L. Genes Dev Resource/Methodology Despite having high-resolution structures for eukaryotic large ribosomal subunits, it remained unclear how these ribonucleoprotein complexes are constructed in living cells. Nevertheless, knowing where ribosomal proteins interact with ribosomal RNA (rRNA) provides a strategic platform to investigate the connection between spatial and temporal aspects of 60S subunit biogenesis. We previously found that the function of individual yeast large subunit ribosomal proteins (RPLs) in precursor rRNA (pre-rRNA) processing correlates with their location in the structure of mature 60S subunits. This observation suggested that there is an order by which 60S subunits are formed. To test this model, we used proteomic approaches to assay changes in the levels of ribosomal proteins and assembly factors in preribosomes when RPLs functioning in early, middle, and late steps of pre-60S assembly are depleted. Our results demonstrate that structural domains of eukaryotic 60S ribosomal subunits are formed in a hierarchical fashion. Assembly begins at the convex solvent side, followed by the polypeptide exit tunnel, the intersubunit side, and finally the central protuberance. This model provides an initial paradigm for the sequential assembly of eukaryotic 60S subunits. Our results reveal striking differences and similarities between assembly of bacterial and eukaryotic large ribosomal subunits, providing insights into how these RNA–protein particles evolved. Cold Spring Harbor Laboratory Press 2014-01-15 /pmc/articles/PMC3909792/ /pubmed/24449272 http://dx.doi.org/10.1101/gad.228825.113 Text en © 2014 Gamalinda et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by-nc/3.0/ This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/. |
spellingShingle | Resource/Methodology Gamalinda, Michael Ohmayer, Uli Jakovljevic, Jelena Kumcuoglu, Beril Woolford, Joshua Mbom, Bertrade Lin, Lawrence Woolford, John L. A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains |
title | A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains |
title_full | A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains |
title_fullStr | A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains |
title_full_unstemmed | A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains |
title_short | A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains |
title_sort | hierarchical model for assembly of eukaryotic 60s ribosomal subunit domains |
topic | Resource/Methodology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909792/ https://www.ncbi.nlm.nih.gov/pubmed/24449272 http://dx.doi.org/10.1101/gad.228825.113 |
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