Functional and structural analysis of maize Hsp101 IRES

© 2014 Jiménez-González et al. Maize heat shock protein of 101 KDa (HSP101) is essential for thermotolerance induction in this plant. The mRNA encoding this protein harbors an IRES element in the 5′UTR that mediates cap-independent translation initiation. In the current work it is demonstrated that...

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Authors: Jiménez-González, Augusto S., Fernández, Noemí, Martínez-Salas, Encarnación, Sánchez de Jiménez, Estela
Format: article
Status:Published version
Publication Date:2014
Country:España
Institution:Consejo Superior de Investigaciones Científicas (CSIC)
Repository:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/124606
Online Access:http://hdl.handle.net/10261/124606
Access Level:Open access
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spelling Functional and structural analysis of maize Hsp101 IRESJiménez-González, Augusto S.Fernández, NoemíMartínez-Salas, EncarnaciónSánchez de Jiménez, Estela© 2014 Jiménez-González et al. Maize heat shock protein of 101 KDa (HSP101) is essential for thermotolerance induction in this plant. The mRNA encoding this protein harbors an IRES element in the 5′UTR that mediates cap-independent translation initiation. In the current work it is demonstrated that hsp101 IRES comprises the entire 5′UTR sequence (150 nts), since deletion of 17 nucleotides from the 5′ end decreased translation efficiency by 87% compared to the control sequence. RNA structure analysis of maize hsp101 IRES revealed the presence of three stem-loops toward its 5′ end, whereas the remainder sequence contains a great proportion of unpaired nucleotides. Furthermore, HSP90 protein was identified by mass spectrometry as the protein preferentially associated with the maize hsp101 IRES. In addition, it has been found that eIFiso4G rather than eIF4G initiation factor mediates translation of the maize hsp101 mRNA.Dereuio´n General de Apoyo al Personal Academico (DGAPA), UNAM, grant IN212910, CONACyT Me´xico scholarship 173696, and Ministerio de Economia y Competitividad (MINECO), grant BFU2011-25437.Peer ReviewedPublic Library of ScienceUniversidad Nacional Autónoma de MéxicoMinisterio de Economía y Competitividad (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2015201520142015info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/124606reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1246062026-05-22T06:33:51Z
dc.title.none.fl_str_mv Functional and structural analysis of maize Hsp101 IRES
title Functional and structural analysis of maize Hsp101 IRES
spellingShingle Functional and structural analysis of maize Hsp101 IRES
Jiménez-González, Augusto S.
title_short Functional and structural analysis of maize Hsp101 IRES
title_full Functional and structural analysis of maize Hsp101 IRES
title_fullStr Functional and structural analysis of maize Hsp101 IRES
title_full_unstemmed Functional and structural analysis of maize Hsp101 IRES
title_sort Functional and structural analysis of maize Hsp101 IRES
dc.creator.none.fl_str_mv Jiménez-González, Augusto S.
Fernández, Noemí
Martínez-Salas, Encarnación
Sánchez de Jiménez, Estela
author Jiménez-González, Augusto S.
author_facet Jiménez-González, Augusto S.
Fernández, Noemí
Martínez-Salas, Encarnación
Sánchez de Jiménez, Estela
author_role author
author2 Fernández, Noemí
Martínez-Salas, Encarnación
Sánchez de Jiménez, Estela
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidad Nacional Autónoma de México
Ministerio de Economía y Competitividad (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description © 2014 Jiménez-González et al. Maize heat shock protein of 101 KDa (HSP101) is essential for thermotolerance induction in this plant. The mRNA encoding this protein harbors an IRES element in the 5′UTR that mediates cap-independent translation initiation. In the current work it is demonstrated that hsp101 IRES comprises the entire 5′UTR sequence (150 nts), since deletion of 17 nucleotides from the 5′ end decreased translation efficiency by 87% compared to the control sequence. RNA structure analysis of maize hsp101 IRES revealed the presence of three stem-loops toward its 5′ end, whereas the remainder sequence contains a great proportion of unpaired nucleotides. Furthermore, HSP90 protein was identified by mass spectrometry as the protein preferentially associated with the maize hsp101 IRES. In addition, it has been found that eIFiso4G rather than eIF4G initiation factor mediates translation of the maize hsp101 mRNA.
publishDate 2014
dc.date.none.fl_str_mv 2014
2015
2015
2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
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dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/124606
url http://hdl.handle.net/10261/124606
dc.language.none.fl_str_mv Inglés
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dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
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