Structural and functional diversity of glutaredoxins in yeast

Glutaredoxins are defined as thiol disulfide oxidoreductases that reduce disulfide bonds employing reduced glutathione as electron donor. They constitute a complex family of proteins with a diversity of enzymatic and functional properties. Thus, dithiol glutaredoxins are able to reduce disulfide bon...

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Autores: Herrero Perpiñán, Enrique, Bellí i Martínez, Gemma, Casas Herranz, Celia
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2010
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:10459.1/47445
Acceso en línea:https://doi.org/10.2174/138920310794557637
http://hdl.handle.net/10459.1/47445
Access Level:acceso abierto
Palabra clave:Glutaredoxin
Estrès oxidatiu
Llevat de cervesa
Saccharomyces cerevisiae
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repository_id_str
spelling Structural and functional diversity of glutaredoxins in yeastHerrero Perpiñán, EnriqueBellí i Martínez, GemmaCasas Herranz, CeliaGlutaredoxinEstrès oxidatiuLlevat de cervesaEstrès oxidatiuSaccharomyces cerevisiaeGlutaredoxins are defined as thiol disulfide oxidoreductases that reduce disulfide bonds employing reduced glutathione as electron donor. They constitute a complex family of proteins with a diversity of enzymatic and functional properties. Thus, dithiol glutaredoxins are able to reduce disulfide bonds and deglutathionylate mixed disulfides between glutathione and cysteine protein residues. They could act regulating the redox state of sulfhydryl residues of specific proteins, while thioredoxins (another family of thiol disulfide oxidoreductases which employ NADPH as electron donor) would be the general sulfhydryl reductants. Some dithiol glutaredoxins such as human Grx2 form dimers bridged by one iron-sulfur cluster, which acts as a sensor of oxidative stress, therefore regulating the activity of the glutaredoxin. The ability to interact with iron-sulfur clusters as ligands is also characteristic of monothiol glutaredoxins with a CGFS-type active site. These do not display thiol oxidoreductase activity, but have roles in iron homeostasis. The three members of this subfamily in Saccharomyces cerevisiae participate in the synthesis of the iron-sulfur clusters in mitochondria (Grx5), or in signalling the iron status inside the cell for regulation of iron uptake and intracellular iron relocalization (Grx3 and Grx4). Such role in iron metabolism seems to be evolutionary conserved. Fungal cells also contain membraneassociated glutaredoxins structurally and enzymatically similar to dithiol glutaredoxins, which may act as redox regulators at the early stages of the protein secretory machinery.Bentham Science Publishers2010info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionhttps://doi.org/10.2174/138920310794557637http://hdl.handle.net/10459.1/47445reponame: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/10.2174/138920310794557637Current protein & peptide science, 2010, vol. 11, núm. 8, p. 659-668(c) Bentham Science Publishersinfo:eu-repo/semantics/openAccessoai:recercat.cat:10459.1/474452026-05-29T05:05:01Z
dc.title.none.fl_str_mv Structural and functional diversity of glutaredoxins in yeast
title Structural and functional diversity of glutaredoxins in yeast
spellingShingle Structural and functional diversity of glutaredoxins in yeast
Herrero Perpiñán, Enrique
Glutaredoxin
Estrès oxidatiu
Llevat de cervesa
Estrès oxidatiu
Saccharomyces cerevisiae
title_short Structural and functional diversity of glutaredoxins in yeast
title_full Structural and functional diversity of glutaredoxins in yeast
title_fullStr Structural and functional diversity of glutaredoxins in yeast
title_full_unstemmed Structural and functional diversity of glutaredoxins in yeast
title_sort Structural and functional diversity of glutaredoxins in yeast
dc.creator.none.fl_str_mv Herrero Perpiñán, Enrique
Bellí i Martínez, Gemma
Casas Herranz, Celia
author Herrero Perpiñán, Enrique
author_facet Herrero Perpiñán, Enrique
Bellí i Martínez, Gemma
Casas Herranz, Celia
author_role author
author2 Bellí i Martínez, Gemma
Casas Herranz, Celia
author2_role 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 are defined as thiol disulfide oxidoreductases that reduce disulfide bonds employing reduced glutathione as electron donor. They constitute a complex family of proteins with a diversity of enzymatic and functional properties. Thus, dithiol glutaredoxins are able to reduce disulfide bonds and deglutathionylate mixed disulfides between glutathione and cysteine protein residues. They could act regulating the redox state of sulfhydryl residues of specific proteins, while thioredoxins (another family of thiol disulfide oxidoreductases which employ NADPH as electron donor) would be the general sulfhydryl reductants. Some dithiol glutaredoxins such as human Grx2 form dimers bridged by one iron-sulfur cluster, which acts as a sensor of oxidative stress, therefore regulating the activity of the glutaredoxin. The ability to interact with iron-sulfur clusters as ligands is also characteristic of monothiol glutaredoxins with a CGFS-type active site. These do not display thiol oxidoreductase activity, but have roles in iron homeostasis. The three members of this subfamily in Saccharomyces cerevisiae participate in the synthesis of the iron-sulfur clusters in mitochondria (Grx5), or in signalling the iron status inside the cell for regulation of iron uptake and intracellular iron relocalization (Grx3 and Grx4). Such role in iron metabolism seems to be evolutionary conserved. Fungal cells also contain membraneassociated glutaredoxins structurally and enzymatically similar to dithiol glutaredoxins, which may act as redox regulators at the early stages of the protein secretory machinery.
publishDate 2010
dc.date.none.fl_str_mv 2010
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/10.2174/138920310794557637
http://hdl.handle.net/10459.1/47445
url https://doi.org/10.2174/138920310794557637
http://hdl.handle.net/10459.1/47445
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/10.2174/138920310794557637
Current protein & peptide science, 2010, vol. 11, núm. 8, p. 659-668
dc.rights.none.fl_str_mv (c) Bentham Science Publishers
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Bentham Science Publishers
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Bentham Science Publishers
publisher.none.fl_str_mv Bentham Science Publishers
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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