Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage

Autores
Irazusta, Verónica Patricia; Obis, Elia; Moreno Cermeño, Armando; Cabiscol, Elisa; Ros, Joaquim; Tamarit, Jordi
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Iron overload is involved in several pathological conditions, including Friedreich ataxia, a disease caused by decreased expression of the mitochondrial protein frataxin. In a previous study, we identified 14 proteins selectively oxidized in yeast cells lacking Yfh1, the yeast frataxin homolog. Most of these were magnesium-binding proteins. Decreased Mn-SOD activity, oxidative damage to CuZn-SOD, and increased levels of chelatable iron were also observed in this model. This study explores the relationship between low SOD activity, the presence of chelatable iron, and protein damage. We observed that addition of copper and manganese to the culture medium restored SOD activity and prevented both oxidative damage and inactivation of magnesium-binding proteins. This protection was compartment specific: recovery of mitochondrial enzymes required the addition of manganese, whereas cytosolic enzymes were recovered by adding copper. Copper treatment also decreased Δyfh1 sensitivity to menadione. Finally, a Δsod1 mutant showed high levels of chelatable iron and inactivation of magnesium-binding enzymes. These results suggest that reduced superoxide dismutase activity contributes to the toxic effects of iron overloading. This would also apply to pathologies involving iron accumulation.
Fil: Irazusta, Verónica Patricia. Universidad de Lleida; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Obis, Elia. Universidad de Lleida; España
Fil: Moreno Cermeño, Armando. Universidad de Lleida; España
Fil: Cabiscol, Elisa. Universidad de Lleida; España
Fil: Ros, Joaquim. Universidad de Lleida; España
Fil: Tamarit, Jordi. Universidad de Lleida; España
Materia
Iron Overload
Protein Carbonylation
Metal Catalyzed-Oxidation
Frataxin
Yeast
Superoxide Dismutase
Iron Toxicity
Friedreich Ataxia
Free Radicals
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/41438
Acceder
id CONICETDig_dca08cfb8481360f51794468e456a846
oai_identifier_str oai:ri.conicet.gov.ar:11336/41438
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damageIrazusta, Verónica PatriciaObis, EliaMoreno Cermeño, ArmandoCabiscol, ElisaRos, JoaquimTamarit, JordiIron OverloadProtein CarbonylationMetal Catalyzed-OxidationFrataxinYeastSuperoxide DismutaseIron ToxicityFriedreich AtaxiaFree Radicalshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Iron overload is involved in several pathological conditions, including Friedreich ataxia, a disease caused by decreased expression of the mitochondrial protein frataxin. In a previous study, we identified 14 proteins selectively oxidized in yeast cells lacking Yfh1, the yeast frataxin homolog. Most of these were magnesium-binding proteins. Decreased Mn-SOD activity, oxidative damage to CuZn-SOD, and increased levels of chelatable iron were also observed in this model. This study explores the relationship between low SOD activity, the presence of chelatable iron, and protein damage. We observed that addition of copper and manganese to the culture medium restored SOD activity and prevented both oxidative damage and inactivation of magnesium-binding proteins. This protection was compartment specific: recovery of mitochondrial enzymes required the addition of manganese, whereas cytosolic enzymes were recovered by adding copper. Copper treatment also decreased Δyfh1 sensitivity to menadione. Finally, a Δsod1 mutant showed high levels of chelatable iron and inactivation of magnesium-binding enzymes. These results suggest that reduced superoxide dismutase activity contributes to the toxic effects of iron overloading. This would also apply to pathologies involving iron accumulation.Fil: Irazusta, Verónica Patricia. Universidad de Lleida; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Obis, Elia. Universidad de Lleida; EspañaFil: Moreno Cermeño, Armando. Universidad de Lleida; EspañaFil: Cabiscol, Elisa. Universidad de Lleida; EspañaFil: Ros, Joaquim. Universidad de Lleida; EspañaFil: Tamarit, Jordi. Universidad de Lleida; EspañaElsevier Science Inc2010-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/41438Irazusta, Verónica Patricia; Obis, Elia; Moreno Cermeño, Armando; Cabiscol, Elisa; Ros, Joaquim; et al.; Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage; Elsevier Science Inc; Free Radical Biology and Medicine; 48; 3; 1-2-2010; 411-4200891-5849CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2009.11.010info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:21:45Zoai:ri.conicet.gov.ar:11336/41438instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:21:45.417CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
title Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
spellingShingle Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
Irazusta, Verónica Patricia
Iron Overload
Protein Carbonylation
Metal Catalyzed-Oxidation
Frataxin
Yeast
Superoxide Dismutase
Iron Toxicity
Friedreich Ataxia
Free Radicals
title_short Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
title_full Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
title_fullStr Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
title_full_unstemmed Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
title_sort Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
dc.creator.none.fl_str_mv Irazusta, Verónica Patricia
Obis, Elia
Moreno Cermeño, Armando
Cabiscol, Elisa
Ros, Joaquim
Tamarit, Jordi
author Irazusta, Verónica Patricia
author_facet Irazusta, Verónica Patricia
Obis, Elia
Moreno Cermeño, Armando
Cabiscol, Elisa
Ros, Joaquim
Tamarit, Jordi
author_role author
author2 Obis, Elia
Moreno Cermeño, Armando
Cabiscol, Elisa
Ros, Joaquim
Tamarit, Jordi
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Iron Overload
Protein Carbonylation
Metal Catalyzed-Oxidation
Frataxin
Yeast
Superoxide Dismutase
Iron Toxicity
Friedreich Ataxia
Free Radicals
topic Iron Overload
Protein Carbonylation
Metal Catalyzed-Oxidation
Frataxin
Yeast
Superoxide Dismutase
Iron Toxicity
Friedreich Ataxia
Free Radicals
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Iron overload is involved in several pathological conditions, including Friedreich ataxia, a disease caused by decreased expression of the mitochondrial protein frataxin. In a previous study, we identified 14 proteins selectively oxidized in yeast cells lacking Yfh1, the yeast frataxin homolog. Most of these were magnesium-binding proteins. Decreased Mn-SOD activity, oxidative damage to CuZn-SOD, and increased levels of chelatable iron were also observed in this model. This study explores the relationship between low SOD activity, the presence of chelatable iron, and protein damage. We observed that addition of copper and manganese to the culture medium restored SOD activity and prevented both oxidative damage and inactivation of magnesium-binding proteins. This protection was compartment specific: recovery of mitochondrial enzymes required the addition of manganese, whereas cytosolic enzymes were recovered by adding copper. Copper treatment also decreased Δyfh1 sensitivity to menadione. Finally, a Δsod1 mutant showed high levels of chelatable iron and inactivation of magnesium-binding enzymes. These results suggest that reduced superoxide dismutase activity contributes to the toxic effects of iron overloading. This would also apply to pathologies involving iron accumulation.
Fil: Irazusta, Verónica Patricia. Universidad de Lleida; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Obis, Elia. Universidad de Lleida; España
Fil: Moreno Cermeño, Armando. Universidad de Lleida; España
Fil: Cabiscol, Elisa. Universidad de Lleida; España
Fil: Ros, Joaquim. Universidad de Lleida; España
Fil: Tamarit, Jordi. Universidad de Lleida; España
description Iron overload is involved in several pathological conditions, including Friedreich ataxia, a disease caused by decreased expression of the mitochondrial protein frataxin. In a previous study, we identified 14 proteins selectively oxidized in yeast cells lacking Yfh1, the yeast frataxin homolog. Most of these were magnesium-binding proteins. Decreased Mn-SOD activity, oxidative damage to CuZn-SOD, and increased levels of chelatable iron were also observed in this model. This study explores the relationship between low SOD activity, the presence of chelatable iron, and protein damage. We observed that addition of copper and manganese to the culture medium restored SOD activity and prevented both oxidative damage and inactivation of magnesium-binding proteins. This protection was compartment specific: recovery of mitochondrial enzymes required the addition of manganese, whereas cytosolic enzymes were recovered by adding copper. Copper treatment also decreased Δyfh1 sensitivity to menadione. Finally, a Δsod1 mutant showed high levels of chelatable iron and inactivation of magnesium-binding enzymes. These results suggest that reduced superoxide dismutase activity contributes to the toxic effects of iron overloading. This would also apply to pathologies involving iron accumulation.
publishDate 2010
dc.date.none.fl_str_mv 2010-02-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/41438
Irazusta, Verónica Patricia; Obis, Elia; Moreno Cermeño, Armando; Cabiscol, Elisa; Ros, Joaquim; et al.; Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage; Elsevier Science Inc; Free Radical Biology and Medicine; 48; 3; 1-2-2010; 411-420
0891-5849
CONICET Digital
CONICET
url http://hdl.handle.net/11336/41438
identifier_str_mv Irazusta, Verónica Patricia; Obis, Elia; Moreno Cermeño, Armando; Cabiscol, Elisa; Ros, Joaquim; et al.; Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage; Elsevier Science Inc; Free Radical Biology and Medicine; 48; 3; 1-2-2010; 411-420
0891-5849
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2009.11.010
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846083365366661120
score 13.22299

Publicaciones similares