Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline
- Autores
- Agüero, Tristán Horacio; Jin, Zhigang; Owens, Dawn; Malhotra, Arun; Newman, Karen; Yang, Jing; King, Mary Lou
- Año de publicación
- 2018
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Dead-end1 expression is restricted to the vertebrate germline where it is believed to activate translation of mRNAs required to protect and promote that unique lineage. nanos1 is one such germline mRNA whose translation is blocked by a secondary mRNA structure within the ORF. Dead-end1 contains a canonical mRNA Recognition Motif (RRM1) in its N-terminus but also contains a less conserved RRM2. Here we provide a mechanistic picture of the nanos1 mRNA-Dead-end1 interaction in the Xenopus germline. We show that RRM1, but not RRM2, is required for binding nanos1. Similar to the zebrafish homologue, Xenopus Dead-end1 possesses ATPase activity. Surprisingly, this activity appears to be within the RRM2, different from the C-terminal region where it is found in zebrafish. More importantly, we show that RRM2 is required for nanos1 translation and germline survival. Further, Dead-end1 functions as a homodimer and binds nanos1 mRNA just downstream of the secondary structure required for nanos1 repression. We propose a model in which the RRM1 is required to bind nanos1 mRNA while the RRM2 is required to promote translation through the action of ATPase. Dead-end1 appears to use RRMs to mimic the function of helicases.
Fil: Agüero, Tristán Horacio. University of Miami; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Jin, Zhigang. University of Illinois; Estados Unidos
Fil: Owens, Dawn. University of Miami; Estados Unidos
Fil: Malhotra, Arun. University of Miami; Estados Unidos
Fil: Newman, Karen. University of Miami; Estados Unidos
Fil: Yang, Jing. University of Miami; Estados Unidos
Fil: King, Mary Lou. University of Miami; Estados Unidos - Materia
-
GERMLINE DEVELOPMENT
DEAD-END1
NANOS1
HELICASE
TRANSLATIONAL REGULATION
XENOPUS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/101740
Ver los metadatos del registro completo
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Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germlineAgüero, Tristán HoracioJin, ZhigangOwens, DawnMalhotra, ArunNewman, KarenYang, JingKing, Mary LouGERMLINE DEVELOPMENTDEAD-END1NANOS1HELICASETRANSLATIONAL REGULATIONXENOPUShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Dead-end1 expression is restricted to the vertebrate germline where it is believed to activate translation of mRNAs required to protect and promote that unique lineage. nanos1 is one such germline mRNA whose translation is blocked by a secondary mRNA structure within the ORF. Dead-end1 contains a canonical mRNA Recognition Motif (RRM1) in its N-terminus but also contains a less conserved RRM2. Here we provide a mechanistic picture of the nanos1 mRNA-Dead-end1 interaction in the Xenopus germline. We show that RRM1, but not RRM2, is required for binding nanos1. Similar to the zebrafish homologue, Xenopus Dead-end1 possesses ATPase activity. Surprisingly, this activity appears to be within the RRM2, different from the C-terminal region where it is found in zebrafish. More importantly, we show that RRM2 is required for nanos1 translation and germline survival. Further, Dead-end1 functions as a homodimer and binds nanos1 mRNA just downstream of the secondary structure required for nanos1 repression. We propose a model in which the RRM1 is required to bind nanos1 mRNA while the RRM2 is required to promote translation through the action of ATPase. Dead-end1 appears to use RRMs to mimic the function of helicases.Fil: Agüero, Tristán Horacio. University of Miami; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Jin, Zhigang. University of Illinois; Estados UnidosFil: Owens, Dawn. University of Miami; Estados UnidosFil: Malhotra, Arun. University of Miami; Estados UnidosFil: Newman, Karen. University of Miami; Estados UnidosFil: Yang, Jing. University of Miami; Estados UnidosFil: King, Mary Lou. University of Miami; Estados UnidosWiley2018-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/101740Agüero, Tristán Horacio; Jin, Zhigang; Owens, Dawn; Malhotra, Arun; Newman, Karen; et al.; Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline; Wiley; Molecular Reproduction and Development; 85; 12; 12-2018; 896-9081040-452X1098-2795CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/mrd.23062info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/mrd.23062info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:24:00Zoai:ri.conicet.gov.ar:11336/101740instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:24:00.919CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline |
title |
Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline |
spellingShingle |
Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline Agüero, Tristán Horacio GERMLINE DEVELOPMENT DEAD-END1 NANOS1 HELICASE TRANSLATIONAL REGULATION XENOPUS |
title_short |
Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline |
title_full |
Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline |
title_fullStr |
Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline |
title_full_unstemmed |
Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline |
title_sort |
Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline |
dc.creator.none.fl_str_mv |
Agüero, Tristán Horacio Jin, Zhigang Owens, Dawn Malhotra, Arun Newman, Karen Yang, Jing King, Mary Lou |
author |
Agüero, Tristán Horacio |
author_facet |
Agüero, Tristán Horacio Jin, Zhigang Owens, Dawn Malhotra, Arun Newman, Karen Yang, Jing King, Mary Lou |
author_role |
author |
author2 |
Jin, Zhigang Owens, Dawn Malhotra, Arun Newman, Karen Yang, Jing King, Mary Lou |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
GERMLINE DEVELOPMENT DEAD-END1 NANOS1 HELICASE TRANSLATIONAL REGULATION XENOPUS |
topic |
GERMLINE DEVELOPMENT DEAD-END1 NANOS1 HELICASE TRANSLATIONAL REGULATION XENOPUS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Dead-end1 expression is restricted to the vertebrate germline where it is believed to activate translation of mRNAs required to protect and promote that unique lineage. nanos1 is one such germline mRNA whose translation is blocked by a secondary mRNA structure within the ORF. Dead-end1 contains a canonical mRNA Recognition Motif (RRM1) in its N-terminus but also contains a less conserved RRM2. Here we provide a mechanistic picture of the nanos1 mRNA-Dead-end1 interaction in the Xenopus germline. We show that RRM1, but not RRM2, is required for binding nanos1. Similar to the zebrafish homologue, Xenopus Dead-end1 possesses ATPase activity. Surprisingly, this activity appears to be within the RRM2, different from the C-terminal region where it is found in zebrafish. More importantly, we show that RRM2 is required for nanos1 translation and germline survival. Further, Dead-end1 functions as a homodimer and binds nanos1 mRNA just downstream of the secondary structure required for nanos1 repression. We propose a model in which the RRM1 is required to bind nanos1 mRNA while the RRM2 is required to promote translation through the action of ATPase. Dead-end1 appears to use RRMs to mimic the function of helicases. Fil: Agüero, Tristán Horacio. University of Miami; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Jin, Zhigang. University of Illinois; Estados Unidos Fil: Owens, Dawn. University of Miami; Estados Unidos Fil: Malhotra, Arun. University of Miami; Estados Unidos Fil: Newman, Karen. University of Miami; Estados Unidos Fil: Yang, Jing. University of Miami; Estados Unidos Fil: King, Mary Lou. University of Miami; Estados Unidos |
description |
Dead-end1 expression is restricted to the vertebrate germline where it is believed to activate translation of mRNAs required to protect and promote that unique lineage. nanos1 is one such germline mRNA whose translation is blocked by a secondary mRNA structure within the ORF. Dead-end1 contains a canonical mRNA Recognition Motif (RRM1) in its N-terminus but also contains a less conserved RRM2. Here we provide a mechanistic picture of the nanos1 mRNA-Dead-end1 interaction in the Xenopus germline. We show that RRM1, but not RRM2, is required for binding nanos1. Similar to the zebrafish homologue, Xenopus Dead-end1 possesses ATPase activity. Surprisingly, this activity appears to be within the RRM2, different from the C-terminal region where it is found in zebrafish. More importantly, we show that RRM2 is required for nanos1 translation and germline survival. Further, Dead-end1 functions as a homodimer and binds nanos1 mRNA just downstream of the secondary structure required for nanos1 repression. We propose a model in which the RRM1 is required to bind nanos1 mRNA while the RRM2 is required to promote translation through the action of ATPase. Dead-end1 appears to use RRMs to mimic the function of helicases. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-12 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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://hdl.handle.net/11336/101740 Agüero, Tristán Horacio; Jin, Zhigang; Owens, Dawn; Malhotra, Arun; Newman, Karen; et al.; Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline; Wiley; Molecular Reproduction and Development; 85; 12; 12-2018; 896-908 1040-452X 1098-2795 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/101740 |
identifier_str_mv |
Agüero, Tristán Horacio; Jin, Zhigang; Owens, Dawn; Malhotra, Arun; Newman, Karen; et al.; Combined functions of two RRMs in dead-end1 mimic helicase activity to promote nanos1 translation in the germline; Wiley; Molecular Reproduction and Development; 85; 12; 12-2018; 896-908 1040-452X 1098-2795 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1002/mrd.23062 info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/mrd.23062 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Wiley |
publisher.none.fl_str_mv |
Wiley |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1846082656897335296 |
score |
13.22299 |