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
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/84317

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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling 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
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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