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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
RNA
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.
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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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