Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana
- Autores
- Turowski, Valeria Rosana; Busi, María Victoria; Gomez Casati, Diego Fabian
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- AtNfs1 is the Arabidopsis thaliana mitochondrial homolog of the bacterial cysteine desulfurases NifS and IscS, having an essential role in cellular Fe–S cluster assembly. Homology modeling of AtNfs1m predicts a high global similarity with E. coli IscS showing a full conservation of residues involved in the catalytic site, whereas the chloroplastic AtNfs2 is more similar to the Synechocystis sp. SufS. Pull-down assays showed that the recombinant mature form, AtNfs1m, specifically binds to Arabidopsis frataxin (AtFH). A hysteretic behavior, with a lag phase of several minutes, was observed and hysteretic parameters were affected by pre-incubation with AtFH. Moreover, AtFH modulates AtNfs1m kinetics, increasing Vmax and decreasing the S0.5 value for cysteine. Results suggest that AtFH plays an important role in the early steps of Fe–S cluster formation by regulating AtNfs1 activity in plant mitochondria.
Fil: Turowski, Valeria Rosana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; Argentina
Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; Argentina
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; Argentina - Materia
-
Cysteine Desulfurase
Fe-S Biogenesis
Mitochondria
Arabidopsis - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/15370
Ver los metadatos del registro completo
id |
CONICETDig_a74c3426c693aa46f3076b437159129a |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/15370 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thalianaTurowski, Valeria RosanaBusi, María VictoriaGomez Casati, Diego FabianCysteine DesulfuraseFe-S BiogenesisMitochondriaArabidopsishttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1AtNfs1 is the Arabidopsis thaliana mitochondrial homolog of the bacterial cysteine desulfurases NifS and IscS, having an essential role in cellular Fe–S cluster assembly. Homology modeling of AtNfs1m predicts a high global similarity with E. coli IscS showing a full conservation of residues involved in the catalytic site, whereas the chloroplastic AtNfs2 is more similar to the Synechocystis sp. SufS. Pull-down assays showed that the recombinant mature form, AtNfs1m, specifically binds to Arabidopsis frataxin (AtFH). A hysteretic behavior, with a lag phase of several minutes, was observed and hysteretic parameters were affected by pre-incubation with AtFH. Moreover, AtFH modulates AtNfs1m kinetics, increasing Vmax and decreasing the S0.5 value for cysteine. Results suggest that AtFH plays an important role in the early steps of Fe–S cluster formation by regulating AtNfs1 activity in plant mitochondria.Fil: Turowski, Valeria Rosana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; ArgentinaFil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; ArgentinaFil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; ArgentinaOxford University Press2012-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/15370Turowski, Valeria Rosana; Busi, María Victoria; Gomez Casati, Diego Fabian; Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana; Oxford University Press; Molecular Plant; 5; 5; 9-2012; 1001-10101674-2052enginfo:eu-repo/semantics/altIdentifier/doi/10.1093/mp/sss037info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S167420521460068Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:29:15Zoai:ri.conicet.gov.ar:11336/15370instacron: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 15:29:16.244CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana |
title |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana |
spellingShingle |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana Turowski, Valeria Rosana Cysteine Desulfurase Fe-S Biogenesis Mitochondria Arabidopsis |
title_short |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana |
title_full |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana |
title_fullStr |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana |
title_full_unstemmed |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana |
title_sort |
Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana |
dc.creator.none.fl_str_mv |
Turowski, Valeria Rosana Busi, María Victoria Gomez Casati, Diego Fabian |
author |
Turowski, Valeria Rosana |
author_facet |
Turowski, Valeria Rosana Busi, María Victoria Gomez Casati, Diego Fabian |
author_role |
author |
author2 |
Busi, María Victoria Gomez Casati, Diego Fabian |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Cysteine Desulfurase Fe-S Biogenesis Mitochondria Arabidopsis |
topic |
Cysteine Desulfurase Fe-S Biogenesis Mitochondria Arabidopsis |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
AtNfs1 is the Arabidopsis thaliana mitochondrial homolog of the bacterial cysteine desulfurases NifS and IscS, having an essential role in cellular Fe–S cluster assembly. Homology modeling of AtNfs1m predicts a high global similarity with E. coli IscS showing a full conservation of residues involved in the catalytic site, whereas the chloroplastic AtNfs2 is more similar to the Synechocystis sp. SufS. Pull-down assays showed that the recombinant mature form, AtNfs1m, specifically binds to Arabidopsis frataxin (AtFH). A hysteretic behavior, with a lag phase of several minutes, was observed and hysteretic parameters were affected by pre-incubation with AtFH. Moreover, AtFH modulates AtNfs1m kinetics, increasing Vmax and decreasing the S0.5 value for cysteine. Results suggest that AtFH plays an important role in the early steps of Fe–S cluster formation by regulating AtNfs1 activity in plant mitochondria. Fil: Turowski, Valeria Rosana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; Argentina Fil: Busi, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; Argentina Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina. Universidad Nacional de Rosario; Argentina. Universidad Nacional de San Martín; Argentina |
description |
AtNfs1 is the Arabidopsis thaliana mitochondrial homolog of the bacterial cysteine desulfurases NifS and IscS, having an essential role in cellular Fe–S cluster assembly. Homology modeling of AtNfs1m predicts a high global similarity with E. coli IscS showing a full conservation of residues involved in the catalytic site, whereas the chloroplastic AtNfs2 is more similar to the Synechocystis sp. SufS. Pull-down assays showed that the recombinant mature form, AtNfs1m, specifically binds to Arabidopsis frataxin (AtFH). A hysteretic behavior, with a lag phase of several minutes, was observed and hysteretic parameters were affected by pre-incubation with AtFH. Moreover, AtFH modulates AtNfs1m kinetics, increasing Vmax and decreasing the S0.5 value for cysteine. Results suggest that AtFH plays an important role in the early steps of Fe–S cluster formation by regulating AtNfs1 activity in plant mitochondria. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-09 |
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/11336/15370 Turowski, Valeria Rosana; Busi, María Victoria; Gomez Casati, Diego Fabian; Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana; Oxford University Press; Molecular Plant; 5; 5; 9-2012; 1001-1010 1674-2052 |
url |
http://hdl.handle.net/11336/15370 |
identifier_str_mv |
Turowski, Valeria Rosana; Busi, María Victoria; Gomez Casati, Diego Fabian; Structural and functional studies of the Mitochondrial Cysteine Desulfurase from Arabidopsis thaliana; Oxford University Press; Molecular Plant; 5; 5; 9-2012; 1001-1010 1674-2052 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1093/mp/sss037 info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S167420521460068X |
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 |
Oxford University Press |
publisher.none.fl_str_mv |
Oxford University Press |
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_ |
1846083432533196800 |
score |
13.22299 |