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Insights into the origin of the nuclear localization signals in conserved ribosomal proteins
Eukaryotic ribosomal proteins, unlike their bacterial homologues, possess nuclear localization signals (NLSs) to enter the cell nucleus during ribosome assembly. Here we provide a comprehensive comparison of bacterial and eukaryotic ribosomes to show that NLSs appear in conserved ribosomal proteins...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4490412/ https://www.ncbi.nlm.nih.gov/pubmed/26066547 http://dx.doi.org/10.1038/ncomms8382 |
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author | Melnikov, Sergey Ben-Shem, Adam Yusupova, Gulnara Yusupov, Marat |
author_facet | Melnikov, Sergey Ben-Shem, Adam Yusupova, Gulnara Yusupov, Marat |
author_sort | Melnikov, Sergey |
collection | PubMed |
description | Eukaryotic ribosomal proteins, unlike their bacterial homologues, possess nuclear localization signals (NLSs) to enter the cell nucleus during ribosome assembly. Here we provide a comprehensive comparison of bacterial and eukaryotic ribosomes to show that NLSs appear in conserved ribosomal proteins via remodelling of their RNA-binding domains. This finding enabled us to identify previously unknown NLSs in ribosomal proteins from humans, and suggests that, apart from promoting protein transport, NLSs may facilitate folding of ribosomal RNA. |
format | Online Article Text |
id | pubmed-4490412 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Pub. Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-44904122015-07-13 Insights into the origin of the nuclear localization signals in conserved ribosomal proteins Melnikov, Sergey Ben-Shem, Adam Yusupova, Gulnara Yusupov, Marat Nat Commun Article Eukaryotic ribosomal proteins, unlike their bacterial homologues, possess nuclear localization signals (NLSs) to enter the cell nucleus during ribosome assembly. Here we provide a comprehensive comparison of bacterial and eukaryotic ribosomes to show that NLSs appear in conserved ribosomal proteins via remodelling of their RNA-binding domains. This finding enabled us to identify previously unknown NLSs in ribosomal proteins from humans, and suggests that, apart from promoting protein transport, NLSs may facilitate folding of ribosomal RNA. Nature Pub. Group 2015-06-11 /pmc/articles/PMC4490412/ /pubmed/26066547 http://dx.doi.org/10.1038/ncomms8382 Text en Copyright © 2015, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Melnikov, Sergey Ben-Shem, Adam Yusupova, Gulnara Yusupov, Marat Insights into the origin of the nuclear localization signals in conserved ribosomal proteins |
title | Insights into the origin of the nuclear localization signals in conserved ribosomal proteins |
title_full | Insights into the origin of the nuclear localization signals in conserved ribosomal proteins |
title_fullStr | Insights into the origin of the nuclear localization signals in conserved ribosomal proteins |
title_full_unstemmed | Insights into the origin of the nuclear localization signals in conserved ribosomal proteins |
title_short | Insights into the origin of the nuclear localization signals in conserved ribosomal proteins |
title_sort | insights into the origin of the nuclear localization signals in conserved ribosomal proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4490412/ https://www.ncbi.nlm.nih.gov/pubmed/26066547 http://dx.doi.org/10.1038/ncomms8382 |
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