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Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch
Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the Drosophila nanos mRNA, required for the formation of the anterior–posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) i...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5602113/ https://www.ncbi.nlm.nih.gov/pubmed/28701521 http://dx.doi.org/10.1261/rna.062208.117 |
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author | Götze, Michael Dufourt, Jérémy Ihling, Christian Rammelt, Christiane Pierson, Stephanie Sambrani, Nagraj Temme, Claudia Sinz, Andrea Simonelig, Martine Wahle, Elmar |
author_facet | Götze, Michael Dufourt, Jérémy Ihling, Christian Rammelt, Christiane Pierson, Stephanie Sambrani, Nagraj Temme, Claudia Sinz, Andrea Simonelig, Martine Wahle, Elmar |
author_sort | Götze, Michael |
collection | PubMed |
description | Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the Drosophila nanos mRNA, required for the formation of the anterior–posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) in the nanos 3′ UTR. In a comprehensive mass spectrometric analysis of the SRE-dependent repressor complex, we identified Smaug, Cup, Me31B, Trailer hitch, eIF4E, and PABPC, in agreement with earlier data. As a novel component, the RNA-dependent ATPase Belle (DDX3) was found, and its involvement in deadenylation and repression of nanos was confirmed in vivo. Smaug, Cup, and Belle bound stoichiometrically to the SREs, independently of RNA length. Binding of Me31B and Tral was also SRE-dependent, but their amounts were proportional to the length of the RNA and equimolar to each other. We suggest that “coating” of the RNA by a Me31B•Tral complex may be at the core of repression. |
format | Online Article Text |
id | pubmed-5602113 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-56021132018-10-01 Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch Götze, Michael Dufourt, Jérémy Ihling, Christian Rammelt, Christiane Pierson, Stephanie Sambrani, Nagraj Temme, Claudia Sinz, Andrea Simonelig, Martine Wahle, Elmar RNA Article Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the Drosophila nanos mRNA, required for the formation of the anterior–posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) in the nanos 3′ UTR. In a comprehensive mass spectrometric analysis of the SRE-dependent repressor complex, we identified Smaug, Cup, Me31B, Trailer hitch, eIF4E, and PABPC, in agreement with earlier data. As a novel component, the RNA-dependent ATPase Belle (DDX3) was found, and its involvement in deadenylation and repression of nanos was confirmed in vivo. Smaug, Cup, and Belle bound stoichiometrically to the SREs, independently of RNA length. Binding of Me31B and Tral was also SRE-dependent, but their amounts were proportional to the length of the RNA and equimolar to each other. We suggest that “coating” of the RNA by a Me31B•Tral complex may be at the core of repression. Cold Spring Harbor Laboratory Press 2017-10 /pmc/articles/PMC5602113/ /pubmed/28701521 http://dx.doi.org/10.1261/rna.062208.117 Text en © 2017 Götze et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/. |
spellingShingle | Article Götze, Michael Dufourt, Jérémy Ihling, Christian Rammelt, Christiane Pierson, Stephanie Sambrani, Nagraj Temme, Claudia Sinz, Andrea Simonelig, Martine Wahle, Elmar Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch |
title | Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch |
title_full | Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch |
title_fullStr | Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch |
title_full_unstemmed | Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch |
title_short | Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch |
title_sort | translational repression of the drosophila nanos mrna involves the rna helicase belle and rna coating by me31b and trailer hitch |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5602113/ https://www.ncbi.nlm.nih.gov/pubmed/28701521 http://dx.doi.org/10.1261/rna.062208.117 |
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