Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin

Thioredoxins are a class of evolutionarily conserved proteins that have been demonstrated to play a key role in many cellular processes involving redox reactions. We report here the genetic and biochemical characterization of Caenorhabditis elegans TRX-3, the first metazoan thioredoxin with an intes...

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Autores: Jiménez-Hidalgo, María, Kurz, Cyril Léopold, Pedrajas, José Rafael, Naranjo-Galindo, Francisco José, González-Barrios, María, Cabello, Juan, Saez, Alberto G, Lozano, Encarnacion, Button, Emma L, Veal, Elizabeth A, Fierro-González, Juan Carlos, Swoboda, Peter, Miranda-Vizuete, Antonio
Tipo de recurso: artículo
Fecha de publicación:2014
País:España
Institución:Instituto de Salud Carlos III (ISCIII)
Repositorio:Repisalud
Idioma:inglés
OAI Identifier:oai:repisalud.isciii.es:20.500.12105/19690
Acceso en línea:http://hdl.handle.net/20.500.12105/19690
Access Level:acceso abierto
Palabra clave:Amino Acid Sequence
Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Intestinal Mucosa
Longevity
Organ Specificity
Oxidation-Reduction
Thioredoxins
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spelling Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxinJiménez-Hidalgo, MaríaKurz, Cyril LéopoldPedrajas, José RafaelNaranjo-Galindo, Francisco JoséGonzález-Barrios, MaríaCabello, JuanSaez, Alberto GLozano, EncarnacionButton, Emma LVeal, Elizabeth AFierro-González, Juan CarlosSwoboda, PeterMiranda-Vizuete, AntonioAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsIntestinal MucosaLongevityOrgan SpecificityOxidation-ReductionThioredoxinsThioredoxins are a class of evolutionarily conserved proteins that have been demonstrated to play a key role in many cellular processes involving redox reactions. We report here the genetic and biochemical characterization of Caenorhabditis elegans TRX-3, the first metazoan thioredoxin with an intestine-specific expression pattern. By using green fluorescent protein reporters we have found that TRX-3 is expressed in both the cytoplasm and the nucleus of intestinal cells, with a prominent localization at the apical membrane. Although intestinal function, reproductive capacity, longevity, and resistance of trx-3 loss-of-function mutants to many stresses are indistinguishable from those of wild-type animals, we have observed a slight reduction in size and a minor reduction in the defecation cycle timing of trx-3 mutants. Interestingly, trx-3 is induced upon infection by Photorhabdus luminescens and Candida albicans, and TRX-3 overexpression provides a modest protection against these pathogens. Together, our data indicate that TRX-3 function in the intestine is dispensable for C. elegans development but may be important to fight specific bacterial and fungal infections.ElsevierNational Institutes of Health (Estados Unidos)Instituto de Salud Carlos IIIRegional Government of Andalusia (España)Unión Europea. Fondo Social Europeo (ESF/FSE)Swedish Research CouncilInstitut National de la Santé et de la Recherche Médicale (Francia)Ministère de la recherche et de l’éducation (Francia)Ministerio de Ciencia e Innovación (España)Ministry of Education, Culture, Sports, Science, and Technology (Japón)Universidad de Jaén (España)Rioja Salud Foundation20242024-06-0720142014-03-0120142014-03-01research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfapplication/pdfimage/tiffimage/tiffimage/tiffhttp://hdl.handle.net/20.500.12105/19690reponame:Repisaludinstname:Instituto de Salud Carlos III (ISCIII)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución 4.0 Internacionalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repisalud.isciii.es:20.500.12105/196902026-06-12T12:43:37Z
dc.title.none.fl_str_mv Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin
title Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin
spellingShingle Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin
Jiménez-Hidalgo, María
Amino Acid Sequence
Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Intestinal Mucosa
Longevity
Organ Specificity
Oxidation-Reduction
Thioredoxins
title_short Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin
title_full Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin
title_fullStr Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin
title_full_unstemmed Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin
title_sort Functional characterization of thioredoxin 3 (TRX-3), a Caenorhabditis elegans intestine-specific thioredoxin
dc.creator.none.fl_str_mv Jiménez-Hidalgo, María
Kurz, Cyril Léopold
Pedrajas, José Rafael
Naranjo-Galindo, Francisco José
González-Barrios, María
Cabello, Juan
Saez, Alberto G
Lozano, Encarnacion
Button, Emma L
Veal, Elizabeth A
Fierro-González, Juan Carlos
Swoboda, Peter
Miranda-Vizuete, Antonio
author Jiménez-Hidalgo, María
author_facet Jiménez-Hidalgo, María
Kurz, Cyril Léopold
Pedrajas, José Rafael
Naranjo-Galindo, Francisco José
González-Barrios, María
Cabello, Juan
Saez, Alberto G
Lozano, Encarnacion
Button, Emma L
Veal, Elizabeth A
Fierro-González, Juan Carlos
Swoboda, Peter
Miranda-Vizuete, Antonio
author_role author
author2 Kurz, Cyril Léopold
Pedrajas, José Rafael
Naranjo-Galindo, Francisco José
González-Barrios, María
Cabello, Juan
Saez, Alberto G
Lozano, Encarnacion
Button, Emma L
Veal, Elizabeth A
Fierro-González, Juan Carlos
Swoboda, Peter
Miranda-Vizuete, Antonio
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv National Institutes of Health (Estados Unidos)
Instituto de Salud Carlos III
Regional Government of Andalusia (España)
Unión Europea. Fondo Social Europeo (ESF/FSE)
Swedish Research Council
Institut National de la Santé et de la Recherche Médicale (Francia)
Ministère de la recherche et de l’éducation (Francia)
Ministerio de Ciencia e Innovación (España)
Ministry of Education, Culture, Sports, Science, and Technology (Japón)
Universidad de Jaén (España)
Rioja Salud Foundation
dc.subject.none.fl_str_mv Amino Acid Sequence
Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Intestinal Mucosa
Longevity
Organ Specificity
Oxidation-Reduction
Thioredoxins
topic Amino Acid Sequence
Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Intestinal Mucosa
Longevity
Organ Specificity
Oxidation-Reduction
Thioredoxins
description Thioredoxins are a class of evolutionarily conserved proteins that have been demonstrated to play a key role in many cellular processes involving redox reactions. We report here the genetic and biochemical characterization of Caenorhabditis elegans TRX-3, the first metazoan thioredoxin with an intestine-specific expression pattern. By using green fluorescent protein reporters we have found that TRX-3 is expressed in both the cytoplasm and the nucleus of intestinal cells, with a prominent localization at the apical membrane. Although intestinal function, reproductive capacity, longevity, and resistance of trx-3 loss-of-function mutants to many stresses are indistinguishable from those of wild-type animals, we have observed a slight reduction in size and a minor reduction in the defecation cycle timing of trx-3 mutants. Interestingly, trx-3 is induced upon infection by Photorhabdus luminescens and Candida albicans, and TRX-3 overexpression provides a modest protection against these pathogens. Together, our data indicate that TRX-3 function in the intestine is dispensable for C. elegans development but may be important to fight specific bacterial and fungal infections.
publishDate 2014
dc.date.none.fl_str_mv 2014
2014-03-01
2014
2014-03-01
2024
2024-06-07
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12105/19690
url http://hdl.handle.net/20.500.12105/19690
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 4.0 Internacional
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Atribución 4.0 Internacional
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
image/tiff
image/tiff
image/tiff
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repisalud
instname:Instituto de Salud Carlos III (ISCIII)
instname_str Instituto de Salud Carlos III (ISCIII)
reponame_str Repisalud
collection Repisalud
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869411518649466880
score 15,81155

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