Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos
- Autores
- Hernández, Greco; Vázquez Pianzola, Paula; Sierra, José M.; Rivera Pomar, Rolando Víctor
- Año de publicación
- 2004
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Translation is a sensitive regulatory step during cellular stress and the apoptosis response. Under such conditions, cap-dependent translation is reduced and internal ribosome entry site (IRES)-dependent translation plays a major role. However, many aspects of how mRNAs are translated under stress remain to be elucidated. Here we report that reaper mRNA, a pro-apoptotic gene from Drosophila melanogaster, is translated in a cap-independent manner. In Drosophila mutant embryos devoid of the eukaryotic initiation factor 4E (eIF4E), reaper transcription is induced and apoptosis proceeds. In vitro translation experiments using wild-type and eIF4E mutant embryonic extracts show that reporter mRNA bearing reaper 5′ untranslated region (UTR) is effectively translated in a cap-independent manner. The 5′UTR of reaper exhibits a high degree of similarity with that of Drosophila heat shock protein 70 mRNA, and both display IRES activity. Studies of mRNA association to polysomes in embryos indicate that both reaper and heat shock protein 70 70 mRNAs are recruited to polysomes under apoptosis or thermal stress. Our data suggest that heat shock protein 70 70 and reaper, two antagonizing factors in apoptosis, use a similar mechanism for protein synthesis.
Facultad de Ciencias Exactas - Materia
-
Ciencias Exactas
1(3)67Af
Drosophila
eIF4E
hsp70
IRES-dependent translation
Reaper - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/84317
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Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryosHernández, GrecoVázquez Pianzola, PaulaSierra, José M.Rivera Pomar, Rolando VíctorCiencias Exactas1(3)67AfDrosophilaeIF4Ehsp70IRES-dependent translationReaperTranslation is a sensitive regulatory step during cellular stress and the apoptosis response. Under such conditions, cap-dependent translation is reduced and internal ribosome entry site (IRES)-dependent translation plays a major role. However, many aspects of how mRNAs are translated under stress remain to be elucidated. Here we report that <i>reaper</i> mRNA, a pro-apoptotic gene from <i>Drosophila melanogaster</i>, is translated in a cap-independent manner. In <i>Drosophila</i> mutant embryos devoid of the eukaryotic initiation factor 4E (eIF4E), <i>reaper</i> transcription is induced and apoptosis proceeds. In vitro translation experiments using wild-type and <i>eIF4E</i> mutant embryonic extracts show that reporter mRNA bearing <i>reaper</i> 5′ untranslated region (UTR) is effectively translated in a cap-independent manner. The 5′UTR of <i>reaper</i> exhibits a high degree of similarity with that of <i>Drosophila</i> <i>heat shock protein 70</i> mRNA, and both display IRES activity. Studies of mRNA association to polysomes in embryos indicate that both <i>reaper</i> and <i>heat shock protein 70</i> 70 mRNAs are recruited to polysomes under apoptosis or thermal stress. Our data suggest that <i>heat shock protein 70</i> 70 and <i>reaper</i>, two antagonizing factors in apoptosis, use a similar mechanism for protein synthesis.Facultad de Ciencias Exactas2004info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1783-1797http://sedici.unlp.edu.ar/handle/10915/84317enginfo:eu-repo/semantics/altIdentifier/issn/1355-8382info:eu-repo/semantics/altIdentifier/doi/10.1261/rna.7154104info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:15Zoai:sedici.unlp.edu.ar:10915/84317Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:15.351SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos |
title |
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos |
spellingShingle |
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos Hernández, Greco Ciencias Exactas 1(3)67Af Drosophila eIF4E hsp70 IRES-dependent translation Reaper |
title_short |
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos |
title_full |
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos |
title_fullStr |
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos |
title_full_unstemmed |
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos |
title_sort |
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos |
dc.creator.none.fl_str_mv |
Hernández, Greco Vázquez Pianzola, Paula Sierra, José M. Rivera Pomar, Rolando Víctor |
author |
Hernández, Greco |
author_facet |
Hernández, Greco Vázquez Pianzola, Paula Sierra, José M. Rivera Pomar, Rolando Víctor |
author_role |
author |
author2 |
Vázquez Pianzola, Paula Sierra, José M. Rivera Pomar, Rolando Víctor |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Ciencias Exactas 1(3)67Af Drosophila eIF4E hsp70 IRES-dependent translation Reaper |
topic |
Ciencias Exactas 1(3)67Af Drosophila eIF4E hsp70 IRES-dependent translation Reaper |
dc.description.none.fl_txt_mv |
Translation is a sensitive regulatory step during cellular stress and the apoptosis response. Under such conditions, cap-dependent translation is reduced and internal ribosome entry site (IRES)-dependent translation plays a major role. However, many aspects of how mRNAs are translated under stress remain to be elucidated. Here we report that <i>reaper</i> mRNA, a pro-apoptotic gene from <i>Drosophila melanogaster</i>, is translated in a cap-independent manner. In <i>Drosophila</i> mutant embryos devoid of the eukaryotic initiation factor 4E (eIF4E), <i>reaper</i> transcription is induced and apoptosis proceeds. In vitro translation experiments using wild-type and <i>eIF4E</i> mutant embryonic extracts show that reporter mRNA bearing <i>reaper</i> 5′ untranslated region (UTR) is effectively translated in a cap-independent manner. The 5′UTR of <i>reaper</i> exhibits a high degree of similarity with that of <i>Drosophila</i> <i>heat shock protein 70</i> mRNA, and both display IRES activity. Studies of mRNA association to polysomes in embryos indicate that both <i>reaper</i> and <i>heat shock protein 70</i> 70 mRNAs are recruited to polysomes under apoptosis or thermal stress. Our data suggest that <i>heat shock protein 70</i> 70 and <i>reaper</i>, two antagonizing factors in apoptosis, use a similar mechanism for protein synthesis. Facultad de Ciencias Exactas |
description |
Translation is a sensitive regulatory step during cellular stress and the apoptosis response. Under such conditions, cap-dependent translation is reduced and internal ribosome entry site (IRES)-dependent translation plays a major role. However, many aspects of how mRNAs are translated under stress remain to be elucidated. Here we report that <i>reaper</i> mRNA, a pro-apoptotic gene from <i>Drosophila melanogaster</i>, is translated in a cap-independent manner. In <i>Drosophila</i> mutant embryos devoid of the eukaryotic initiation factor 4E (eIF4E), <i>reaper</i> transcription is induced and apoptosis proceeds. In vitro translation experiments using wild-type and <i>eIF4E</i> mutant embryonic extracts show that reporter mRNA bearing <i>reaper</i> 5′ untranslated region (UTR) is effectively translated in a cap-independent manner. The 5′UTR of <i>reaper</i> exhibits a high degree of similarity with that of <i>Drosophila</i> <i>heat shock protein 70</i> mRNA, and both display IRES activity. Studies of mRNA association to polysomes in embryos indicate that both <i>reaper</i> and <i>heat shock protein 70</i> 70 mRNAs are recruited to polysomes under apoptosis or thermal stress. Our data suggest that <i>heat shock protein 70</i> 70 and <i>reaper</i>, two antagonizing factors in apoptosis, use a similar mechanism for protein synthesis. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/84317 |
url |
http://sedici.unlp.edu.ar/handle/10915/84317 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/1355-8382 info:eu-repo/semantics/altIdentifier/doi/10.1261/rna.7154104 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
dc.format.none.fl_str_mv |
application/pdf 1783-1797 |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
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