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Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes
The cold shock domain is one of the most highly conserved motifs between bacteria and higher eukaryotes. Y-box-binding proteins represent a subfamily of cold shock domain proteins with pleiotropic functions, ranging from transcription in the nucleus to translation in the cytoplasm. These proteins ha...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4245946/ https://www.ncbi.nlm.nih.gov/pubmed/25378320 http://dx.doi.org/10.1093/nar/gku1077 |
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author | Arnold, Andreas Rahman, Md Masuder Lee, Man Chun Muehlhaeusser, Sandra Katic, Iskra Gaidatzis, Dimos Hess, Daniel Scheckel, Claudia Wright, Jane E. Stetak, Attila Boag, Peter R. Ciosk, Rafal |
author_facet | Arnold, Andreas Rahman, Md Masuder Lee, Man Chun Muehlhaeusser, Sandra Katic, Iskra Gaidatzis, Dimos Hess, Daniel Scheckel, Claudia Wright, Jane E. Stetak, Attila Boag, Peter R. Ciosk, Rafal |
author_sort | Arnold, Andreas |
collection | PubMed |
description | The cold shock domain is one of the most highly conserved motifs between bacteria and higher eukaryotes. Y-box-binding proteins represent a subfamily of cold shock domain proteins with pleiotropic functions, ranging from transcription in the nucleus to translation in the cytoplasm. These proteins have been investigated in all major model organisms except Caenorhabditis elegans. In this study, we set out to fill this gap and present a functional characterization of CEYs, the C. elegans Y-box-binding proteins. We find that, similar to other organisms, CEYs are essential for proper gametogenesis. However, we also report a novel function of these proteins in the formation of large polysomes in the soma. In the absence of the somatic CEYs, polysomes are dramatically reduced with a simultaneous increase in monosomes and disomes, which, unexpectedly, has no obvious impact on animal biology. Because transcripts that are enriched in polysomes in wild-type animals tend to be less abundant in the absence of CEYs, our findings suggest that large polysomes might depend on transcript stabilization mediated by CEY proteins. |
format | Online Article Text |
id | pubmed-4245946 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-42459462014-12-01 Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes Arnold, Andreas Rahman, Md Masuder Lee, Man Chun Muehlhaeusser, Sandra Katic, Iskra Gaidatzis, Dimos Hess, Daniel Scheckel, Claudia Wright, Jane E. Stetak, Attila Boag, Peter R. Ciosk, Rafal Nucleic Acids Res RNA The cold shock domain is one of the most highly conserved motifs between bacteria and higher eukaryotes. Y-box-binding proteins represent a subfamily of cold shock domain proteins with pleiotropic functions, ranging from transcription in the nucleus to translation in the cytoplasm. These proteins have been investigated in all major model organisms except Caenorhabditis elegans. In this study, we set out to fill this gap and present a functional characterization of CEYs, the C. elegans Y-box-binding proteins. We find that, similar to other organisms, CEYs are essential for proper gametogenesis. However, we also report a novel function of these proteins in the formation of large polysomes in the soma. In the absence of the somatic CEYs, polysomes are dramatically reduced with a simultaneous increase in monosomes and disomes, which, unexpectedly, has no obvious impact on animal biology. Because transcripts that are enriched in polysomes in wild-type animals tend to be less abundant in the absence of CEYs, our findings suggest that large polysomes might depend on transcript stabilization mediated by CEY proteins. Oxford University Press 2014-12-01 2014-11-05 /pmc/articles/PMC4245946/ /pubmed/25378320 http://dx.doi.org/10.1093/nar/gku1077 Text en © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://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 | RNA Arnold, Andreas Rahman, Md Masuder Lee, Man Chun Muehlhaeusser, Sandra Katic, Iskra Gaidatzis, Dimos Hess, Daniel Scheckel, Claudia Wright, Jane E. Stetak, Attila Boag, Peter R. Ciosk, Rafal Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes |
title | Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes |
title_full | Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes |
title_fullStr | Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes |
title_full_unstemmed | Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes |
title_short | Functional characterization of C. elegans Y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes |
title_sort | functional characterization of c. elegans y-box-binding proteins reveals tissue-specific functions and a critical role in the formation of polysomes |
topic | RNA |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4245946/ https://www.ncbi.nlm.nih.gov/pubmed/25378320 http://dx.doi.org/10.1093/nar/gku1077 |
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