Glutaredoxins in fungi

Glutaredoxins (GRXs) can be subdivided into two subfamilies: dithiol GRXs with the CPY/FC active site motif, and monothiol GRXs with the CGFS motif. Both subfamilies share a thioredoxin-fold structure. Monothiol GRXs exist with a single Grx domain while others have a thioredoxin-like domain (Trx) an...

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Autores: Herrero Perpiñán, Enrique, Ros Salvador, Joaquim, Tamarit Sumalla, Jordi, Bellí i Martínez, Gemma
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2006
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:10459.1/47441
Acceso en línea:https://doi.org/10.1007/s11120-006-9079-3
http://hdl.handle.net/10459.1/47441
Access Level:acceso abierto
Palabra clave:Glutaredoxin
Estrès oxidatiu
Llevat de cervesa
Saccharomyces cerevisiae
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spelling Glutaredoxins in fungiHerrero Perpiñán, EnriqueRos Salvador, JoaquimTamarit Sumalla, JordiBellí i Martínez, GemmaGlutaredoxinEstrès oxidatiuLlevat de cervesaEstrès oxidatiuSaccharomyces cerevisiaeGlutaredoxins (GRXs) can be subdivided into two subfamilies: dithiol GRXs with the CPY/FC active site motif, and monothiol GRXs with the CGFS motif. Both subfamilies share a thioredoxin-fold structure. Monothiol GRXs exist with a single Grx domain while others have a thioredoxin-like domain (Trx) and one or more Grx domains in tandem. Most fungi have both dithiol and monothiol GRXs with different subcellular locations. GRX-like molecules also exist in fungi that separate in one residue from one of the canonical active site motifs. Additionally, Omega-class glutathione transferases are active as GRXs. Among fungi, the GRXs more extensively studied are those from Saccharomyces cerevisiae. This organism contains two dithiol GRXs (ScGrx1 and ScGrx2) with partially overlapping functions in defence against oxidative stress. In this function, they cooperate with glutathione transferases Gtt1 and Gtt2. While ScGrx1 is cytosolic, two pools exist for ScGrx2, a major one at the cytosol and a minor one at mitocondria. On the other hand, S. cerevisiae cells have two monothiol GRXs with the Trx-Grx structure (ScGrx3 and ScGrx4) that locate at the nucleus and probably regulate the activity of transcription factors such as Aft1, and one monothiol glutaredoxin with the Grx structure (ScGrx5) that localizes as the mitochondria matrix, where it participates in the synthesis of iron-sulfur clusters. The function of yeast Grx5 seems to be conserved along the evolutionary scale.Springer2006info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionhttps://doi.org/10.1007/s11120-006-9079-3http://hdl.handle.net/10459.1/47441reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésVersió preprint del document publicat a https://doi.org/10.1007/s11120-006-9079-3Photosynthesis research, 2006, vol. 86, núm. 2-3, p. 127-140(c) Springer Science, 2006(c) Business Media. 2006info:eu-repo/semantics/openAccessoai:recercat.cat:10459.1/474412026-05-29T05:05:01Z
dc.title.none.fl_str_mv Glutaredoxins in fungi
title Glutaredoxins in fungi
spellingShingle Glutaredoxins in fungi
Herrero Perpiñán, Enrique
Glutaredoxin
Estrès oxidatiu
Llevat de cervesa
Estrès oxidatiu
Saccharomyces cerevisiae
title_short Glutaredoxins in fungi
title_full Glutaredoxins in fungi
title_fullStr Glutaredoxins in fungi
title_full_unstemmed Glutaredoxins in fungi
title_sort Glutaredoxins in fungi
dc.creator.none.fl_str_mv Herrero Perpiñán, Enrique
Ros Salvador, Joaquim
Tamarit Sumalla, Jordi
Bellí i Martínez, Gemma
author Herrero Perpiñán, Enrique
author_facet Herrero Perpiñán, Enrique
Ros Salvador, Joaquim
Tamarit Sumalla, Jordi
Bellí i Martínez, Gemma
author_role author
author2 Ros Salvador, Joaquim
Tamarit Sumalla, Jordi
Bellí i Martínez, Gemma
author2_role author
author
author
dc.subject.none.fl_str_mv Glutaredoxin
Estrès oxidatiu
Llevat de cervesa
Estrès oxidatiu
Saccharomyces cerevisiae
topic Glutaredoxin
Estrès oxidatiu
Llevat de cervesa
Estrès oxidatiu
Saccharomyces cerevisiae
description Glutaredoxins (GRXs) can be subdivided into two subfamilies: dithiol GRXs with the CPY/FC active site motif, and monothiol GRXs with the CGFS motif. Both subfamilies share a thioredoxin-fold structure. Monothiol GRXs exist with a single Grx domain while others have a thioredoxin-like domain (Trx) and one or more Grx domains in tandem. Most fungi have both dithiol and monothiol GRXs with different subcellular locations. GRX-like molecules also exist in fungi that separate in one residue from one of the canonical active site motifs. Additionally, Omega-class glutathione transferases are active as GRXs. Among fungi, the GRXs more extensively studied are those from Saccharomyces cerevisiae. This organism contains two dithiol GRXs (ScGrx1 and ScGrx2) with partially overlapping functions in defence against oxidative stress. In this function, they cooperate with glutathione transferases Gtt1 and Gtt2. While ScGrx1 is cytosolic, two pools exist for ScGrx2, a major one at the cytosol and a minor one at mitocondria. On the other hand, S. cerevisiae cells have two monothiol GRXs with the Trx-Grx structure (ScGrx3 and ScGrx4) that locate at the nucleus and probably regulate the activity of transcription factors such as Aft1, and one monothiol glutaredoxin with the Grx structure (ScGrx5) that localizes as the mitochondria matrix, where it participates in the synthesis of iron-sulfur clusters. The function of yeast Grx5 seems to be conserved along the evolutionary scale.
publishDate 2006
dc.date.none.fl_str_mv 2006
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv https://doi.org/10.1007/s11120-006-9079-3
http://hdl.handle.net/10459.1/47441
url https://doi.org/10.1007/s11120-006-9079-3
http://hdl.handle.net/10459.1/47441
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió preprint del document publicat a https://doi.org/10.1007/s11120-006-9079-3
Photosynthesis research, 2006, vol. 86, núm. 2-3, p. 127-140
dc.rights.none.fl_str_mv (c) Springer Science, 2006
(c) Business Media. 2006
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Springer Science, 2006
(c) Business Media. 2006
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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