Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress

In eukaryotic organisms, hydrogen peroxide has a dual effect; it is potentially toxic for the cell but also has an important signaling activity. According to the previously proposed floodgate hypothesis, the signaling activity of hydrogen peroxide in eukaryotes requires a transient increase in its c...

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Autores: Pascual, María B., Mata Cabana, Alejandro, Florencio Bellido, Francisco Javier, Lindahl, Marika, Cejudo Fernández, Francisco Javier
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2010
País:España
Recursos:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/129860
Acesso em linha:https://hdl.handle.net/11441/129860
https://doi.org/10.1074/jbc.M110.160465
Access Level:acceso abierto
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spelling Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stressPascual, María B.Mata Cabana, AlejandroFlorencio Bellido, Francisco JavierLindahl, MarikaCejudo Fernández, Francisco JavierIn eukaryotic organisms, hydrogen peroxide has a dual effect; it is potentially toxic for the cell but also has an important signaling activity. According to the previously proposed floodgate hypothesis, the signaling activity of hydrogen peroxide in eukaryotes requires a transient increase in its concentration, which is due to the inactivation by overoxidation of 2-Cys peroxiredoxin (2-Cys Prx). Sensitivity to overoxidation depends on the structural GGLG and YF motifs present in eukaryotic 2-Cys Prxs and is believed to be absent from prokaryotic enzymes, thus representing a paradoxical gain of function exclusive to eukaryotic organisms. Here we show that 2-Cys Prxs from several prokaryotic organisms, including cyanobacteria, contain the GG(L/ V/I)G and YF motifs characteristic of sensitive enzymes. In search of the existence of overoxidation-sensitive 2-Cys Prxs in prokaryotes, we have analyzed the sensitivity to overoxidation of 2-Cys Prxs from two cyanobacterial strains, Anabaena sp. PCC7120 and Synechocystis sp. PCC6803. In vitro analysis of wild type and mutant variants of the Anabaena 2-Cys Prx showed that this enzyme is overoxidized at the peroxidatic cysteine residue, thus constituting an exception among prokaryotes. Moreover, the 2-Cys Prx from Anabaena is readily and reversibly overoxidized in vivo in response to high light and hydrogen peroxide, showing higher sensitivity to overoxidation than the Synechocystis enzyme. These cyanobacterial strains have different strategies to cope with hydrogen peroxide. While Synechocystis has low content of less sensitive 2-Cys Prx and high catalase activity, Anabaena contains abundant and sensitive 2-Cys Prx, but low catalase activity, which is remarkably similar to the chloroplast system.Ministerio de Educación y Ciencia BIO2007-60644, BFU2007-60300Junta de Andalucía P06-CVI01578, BIO-182, BIO-284ElsevierBioquímica Vegetal y Biología Molecular2010info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/129860https://doi.org/10.1074/jbc.M110.160465reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésJournal of Biological Chemistry, 285 (45), 34485-34492.BIO2007-60644BFU2007-60300P06-CVI01578BIO-182BIO-284https://doi.org/10.1074/jbc.M110.160465info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1298602026-06-17T12:51:07Z
dc.title.none.fl_str_mv Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress
title Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress
spellingShingle Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress
Pascual, María B.
title_short Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress
title_full Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress
title_fullStr Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress
title_full_unstemmed Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress
title_sort Overoxidation of 2-cys peroxiredoxin in prokaryotes: Cyanobacterial 2-cys peroxiredoxins sensitive to oxidative stress
dc.creator.none.fl_str_mv Pascual, María B.
Mata Cabana, Alejandro
Florencio Bellido, Francisco Javier
Lindahl, Marika
Cejudo Fernández, Francisco Javier
author Pascual, María B.
author_facet Pascual, María B.
Mata Cabana, Alejandro
Florencio Bellido, Francisco Javier
Lindahl, Marika
Cejudo Fernández, Francisco Javier
author_role author
author2 Mata Cabana, Alejandro
Florencio Bellido, Francisco Javier
Lindahl, Marika
Cejudo Fernández, Francisco Javier
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
description In eukaryotic organisms, hydrogen peroxide has a dual effect; it is potentially toxic for the cell but also has an important signaling activity. According to the previously proposed floodgate hypothesis, the signaling activity of hydrogen peroxide in eukaryotes requires a transient increase in its concentration, which is due to the inactivation by overoxidation of 2-Cys peroxiredoxin (2-Cys Prx). Sensitivity to overoxidation depends on the structural GGLG and YF motifs present in eukaryotic 2-Cys Prxs and is believed to be absent from prokaryotic enzymes, thus representing a paradoxical gain of function exclusive to eukaryotic organisms. Here we show that 2-Cys Prxs from several prokaryotic organisms, including cyanobacteria, contain the GG(L/ V/I)G and YF motifs characteristic of sensitive enzymes. In search of the existence of overoxidation-sensitive 2-Cys Prxs in prokaryotes, we have analyzed the sensitivity to overoxidation of 2-Cys Prxs from two cyanobacterial strains, Anabaena sp. PCC7120 and Synechocystis sp. PCC6803. In vitro analysis of wild type and mutant variants of the Anabaena 2-Cys Prx showed that this enzyme is overoxidized at the peroxidatic cysteine residue, thus constituting an exception among prokaryotes. Moreover, the 2-Cys Prx from Anabaena is readily and reversibly overoxidized in vivo in response to high light and hydrogen peroxide, showing higher sensitivity to overoxidation than the Synechocystis enzyme. These cyanobacterial strains have different strategies to cope with hydrogen peroxide. While Synechocystis has low content of less sensitive 2-Cys Prx and high catalase activity, Anabaena contains abundant and sensitive 2-Cys Prx, but low catalase activity, which is remarkably similar to the chloroplast system.
publishDate 2010
dc.date.none.fl_str_mv 2010
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/129860
https://doi.org/10.1074/jbc.M110.160465
url https://hdl.handle.net/11441/129860
https://doi.org/10.1074/jbc.M110.160465
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Journal of Biological Chemistry, 285 (45), 34485-34492.
BIO2007-60644
BFU2007-60300
P06-CVI01578
BIO-182
BIO-284
https://doi.org/10.1074/jbc.M110.160465
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
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