Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency

In response to iron deficiency, the budding yeast Saccharomyces cerevisiae undergoes a metabolic remodeling in order to optimize iron utilization. The tandem zinc finger (TZF)-containing protein Cth2 plays a critical role in this adaptation by binding and promoting the degradation of multiple mRNAs...

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Autores: Ramos Alonso, Lucía, Romero, Antonia M., Soler, M.À., Perea García, Ana, Alepuz, Paula, Puig, Sergi, Martínez Pastor, M.Teresa
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/193285
Acceso en línea:http://hdl.handle.net/10261/193285
Access Level:acceso abierto
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spelling Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiencyRamos Alonso, LucíaRomero, Antonia M.Soler, M.À.Perea García, AnaAlepuz, PaulaPuig, SergiMartínez Pastor, M.TeresaIn response to iron deficiency, the budding yeast Saccharomyces cerevisiae undergoes a metabolic remodeling in order to optimize iron utilization. The tandem zinc finger (TZF)-containing protein Cth2 plays a critical role in this adaptation by binding and promoting the degradation of multiple mRNAs that contain AU-rich elements (AREs). Here, we demonstrate that Cth2 also functions as a translational repressor of its target mRNAs. By complementary approaches, we demonstrate that Cth2 protein inhibits the translation of SDH4, which encodes a subunit of succinate dehydrogenase, and CTH2 mRNAs in response to iron depletion. Both the AREs within SDH4 and CTH2 transcripts, and the Cth2 TZF are essential for translational repression. We show that the role played by Cth2 as a negative translational regulator extends to other mRNA targets such as WTM1, CCP1 and HEM15. A structure-function analysis of Cth2 protein suggests that the Cth2 amino-terminal domain (NTD) is important for both mRNA turnover and translation inhibition, while its carboxy-terminal domain (CTD) only participates in the regulation of translation, but is dispensable for mRNA degradation. Finally, we demonstrate that the Cth2 CTD is physiologically relevant for adaptation to iron deficiency.Peer ReviewedPublic Library of ScienceConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2019201920182019info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/193285reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1932852026-05-22T06:33:51Z
dc.title.none.fl_str_mv Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency
title Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency
spellingShingle Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency
Ramos Alonso, Lucía
title_short Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency
title_full Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency
title_fullStr Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency
title_full_unstemmed Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency
title_sort Yeast Cth2 protein represses the translation of ARE-containing mRNAs in response to iron deficiency
dc.creator.none.fl_str_mv Ramos Alonso, Lucía
Romero, Antonia M.
Soler, M.À.
Perea García, Ana
Alepuz, Paula
Puig, Sergi
Martínez Pastor, M.Teresa
author Ramos Alonso, Lucía
author_facet Ramos Alonso, Lucía
Romero, Antonia M.
Soler, M.À.
Perea García, Ana
Alepuz, Paula
Puig, Sergi
Martínez Pastor, M.Teresa
author_role author
author2 Romero, Antonia M.
Soler, M.À.
Perea García, Ana
Alepuz, Paula
Puig, Sergi
Martínez Pastor, M.Teresa
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description In response to iron deficiency, the budding yeast Saccharomyces cerevisiae undergoes a metabolic remodeling in order to optimize iron utilization. The tandem zinc finger (TZF)-containing protein Cth2 plays a critical role in this adaptation by binding and promoting the degradation of multiple mRNAs that contain AU-rich elements (AREs). Here, we demonstrate that Cth2 also functions as a translational repressor of its target mRNAs. By complementary approaches, we demonstrate that Cth2 protein inhibits the translation of SDH4, which encodes a subunit of succinate dehydrogenase, and CTH2 mRNAs in response to iron depletion. Both the AREs within SDH4 and CTH2 transcripts, and the Cth2 TZF are essential for translational repression. We show that the role played by Cth2 as a negative translational regulator extends to other mRNA targets such as WTM1, CCP1 and HEM15. A structure-function analysis of Cth2 protein suggests that the Cth2 amino-terminal domain (NTD) is important for both mRNA turnover and translation inhibition, while its carboxy-terminal domain (CTD) only participates in the regulation of translation, but is dispensable for mRNA degradation. Finally, we demonstrate that the Cth2 CTD is physiologically relevant for adaptation to iron deficiency.
publishDate 2018
dc.date.none.fl_str_mv 2018
2019
2019
2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/193285
url http://hdl.handle.net/10261/193285
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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