The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP

Autores
Ferrero, Diego; Aran, Martin; Rimmaudo, Laura Elizabeth; Wolosiuk, Ricardo Alejandro
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
2-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous enzymes that have been implicated in peroxide-mediated signaling of markedly different processes, such as cancer and photosynthesis. A highly conserved C-terminal extension of eukaryotic homologues modulates both the overoxidation of cysteines and the formation of oligomers. Here, we reveal that the plant counterpart regulates the self-polymerization of 2-Cys Prx triggered by ATP and Mg(2+). This feature is of particular importance under oxidative stress because the interaction of ATP with 2-Cys Prx rapidly integrates nonredox chemistry of signaling pathways into a network hub governed by multiple redox transformations at cysteine residues.
Fil: Ferrero, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Aran, Martin. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Rimmaudo, Laura Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Wolosiuk, Ricardo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Materia
2-Cys Peroxiredoxin
Atp-Binding
Oligomerization
Protein Aggregation
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:11336/8477
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATPFerrero, DiegoAran, MartinRimmaudo, Laura ElizabethWolosiuk, Ricardo Alejandro2-Cys PeroxiredoxinAtp-BindingOligomerizationProtein Aggregationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/12-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous enzymes that have been implicated in peroxide-mediated signaling of markedly different processes, such as cancer and photosynthesis. A highly conserved C-terminal extension of eukaryotic homologues modulates both the overoxidation of cysteines and the formation of oligomers. Here, we reveal that the plant counterpart regulates the self-polymerization of 2-Cys Prx triggered by ATP and Mg(2+). This feature is of particular importance under oxidative stress because the interaction of ATP with 2-Cys Prx rapidly integrates nonredox chemistry of signaling pathways into a network hub governed by multiple redox transformations at cysteine residues.Fil: Ferrero, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Aran, Martin. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Rimmaudo, Laura Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Wolosiuk, Ricardo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; ArgentinaAmerican Chemical Society2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8477Ferrero, Diego; Aran, Martin; Rimmaudo, Laura Elizabeth; Wolosiuk, Ricardo Alejandro; The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP; American Chemical Society; Biochemistry; 51; 11; -1-2012; 2169-21710006-2960enginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/full/10.1021/bi201843binfo:eu-repo/semantics/altIdentifier/doi/10.1021/bi201843binfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:23:22Zoai:ri.conicet.gov.ar:11336/8477instacron: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 15:23:23.126CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP
title The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP
spellingShingle The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP
Ferrero, Diego
2-Cys Peroxiredoxin
Atp-Binding
Oligomerization
Protein Aggregation
title_short The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP
title_full The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP
title_fullStr The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP
title_full_unstemmed The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP
title_sort The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP
dc.creator.none.fl_str_mv Ferrero, Diego
Aran, Martin
Rimmaudo, Laura Elizabeth
Wolosiuk, Ricardo Alejandro
author Ferrero, Diego
author_facet Ferrero, Diego
Aran, Martin
Rimmaudo, Laura Elizabeth
Wolosiuk, Ricardo Alejandro
author_role author
author2 Aran, Martin
Rimmaudo, Laura Elizabeth
Wolosiuk, Ricardo Alejandro
author2_role author
author
author
dc.subject.none.fl_str_mv 2-Cys Peroxiredoxin
Atp-Binding
Oligomerization
Protein Aggregation
topic 2-Cys Peroxiredoxin
Atp-Binding
Oligomerization
Protein Aggregation
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 2-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous enzymes that have been implicated in peroxide-mediated signaling of markedly different processes, such as cancer and photosynthesis. A highly conserved C-terminal extension of eukaryotic homologues modulates both the overoxidation of cysteines and the formation of oligomers. Here, we reveal that the plant counterpart regulates the self-polymerization of 2-Cys Prx triggered by ATP and Mg(2+). This feature is of particular importance under oxidative stress because the interaction of ATP with 2-Cys Prx rapidly integrates nonredox chemistry of signaling pathways into a network hub governed by multiple redox transformations at cysteine residues.
Fil: Ferrero, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Aran, Martin. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Rimmaudo, Laura Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Wolosiuk, Ricardo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina
description 2-Cys peroxiredoxins (2-Cys Prxs) are ubiquitous enzymes that have been implicated in peroxide-mediated signaling of markedly different processes, such as cancer and photosynthesis. A highly conserved C-terminal extension of eukaryotic homologues modulates both the overoxidation of cysteines and the formation of oligomers. Here, we reveal that the plant counterpart regulates the self-polymerization of 2-Cys Prx triggered by ATP and Mg(2+). This feature is of particular importance under oxidative stress because the interaction of ATP with 2-Cys Prx rapidly integrates nonredox chemistry of signaling pathways into a network hub governed by multiple redox transformations at cysteine residues.
publishDate 2012
dc.date.none.fl_str_mv 2012
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/11336/8477
Ferrero, Diego; Aran, Martin; Rimmaudo, Laura Elizabeth; Wolosiuk, Ricardo Alejandro; The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP; American Chemical Society; Biochemistry; 51; 11; -1-2012; 2169-2171
0006-2960
url http://hdl.handle.net/11336/8477
identifier_str_mv Ferrero, Diego; Aran, Martin; Rimmaudo, Laura Elizabeth; Wolosiuk, Ricardo Alejandro; The C-Terminal Extension of Chloroplast 2-Cys Peroxiredoxin is Critical for Interaction with ATP; American Chemical Society; Biochemistry; 51; 11; -1-2012; 2169-2171
0006-2960
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/full/10.1021/bi201843b
info:eu-repo/semantics/altIdentifier/doi/10.1021/bi201843b
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 American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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
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score 13.22299

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