Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism

Autores
Consentino, Laurent; Lambert, Stefan; Martino, Carlos; Jourdan, Nathalie; Bouchet, Pierre Etienne; Witczak, Jacques; Castello, Pablo Raul; El-Esawi, Mohamed; Corbineau, Francoise; d'Harlingue, Alain; Ahmad, Margaret
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cryptochromes are widespread blue-light absorbing flavoproteins with important signaling roles. In plants they mediate de-etiolation, developmental and stress responses resulting from interaction with downstream signaling partners such as transcription factors and components of the proteasome. Recently, it has been shown that Arabidopsis cry1 activation by blue light also results in direct enzymatic conversion of molecular oxygen (O2) to reactive oxygen species (ROS) and hydrogen peroxide (H2O2) in vitro. Here we explored whether direct enzymatic synthesis of ROS by Arabidopsis cry1 can play a physiological role in vivo. ROS formation resulting from cry1 expression was measured by fluorescence assay in insect cell cultures and in Arabidopsis protoplasts from cryptochrome mutant seedlings. Cell death was determined by colorimetric assay. We found that ROS formation results from cry1 activation and induces cell death in insect cell cultures. In plant protoplasts, cryptochrome activation results in rapid increase in ROS formation and cell death. We conclude that ROS formation by cryptochromes may indeed be of physiological relevance and could represent a novel paradigm for cryptochrome signaling.
Fil: Consentino, Laurent. Université Pierre et Marie Curie; Francia
Fil: Lambert, Stefan. Université Pierre et Marie Curie; Francia
Fil: Martino, Carlos. Université Pierre et Marie Curie; Francia. University of Florida; Estados Unidos
Fil: Jourdan, Nathalie. Université Pierre et Marie Curie; Francia
Fil: Bouchet, Pierre Etienne. Université Pierre et Marie Curie; Francia
Fil: Witczak, Jacques. Université Pierre et Marie Curie; Francia
Fil: Castello, Pablo Raul. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Université Pierre et Marie Curie; Francia
Fil: El-Esawi, Mohamed. Université Pierre et Marie Curie; Francia. Tanta University; Egipto
Fil: Corbineau, Francoise. Université Pierre et Marie Curie; Francia
Fil: d'Harlingue, Alain. Université Pierre et Marie Curie; Francia
Fil: Ahmad, Margaret. Université Pierre et Marie Curie; Francia. Universidad Xavier; Estados Unidos
Materia
ARABIDOPSIS THALIANA
CRYPTOCHROME
OXIDATIVE STRESS
PHOTOMORPHOGENESIS
PHOTORECEPTOR
REACTIVE OXYGEN SPECIES (ROS) SIGNALING
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:11336/99292

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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanismConsentino, LaurentLambert, StefanMartino, CarlosJourdan, NathalieBouchet, Pierre EtienneWitczak, JacquesCastello, Pablo RaulEl-Esawi, MohamedCorbineau, Francoised'Harlingue, AlainAhmad, MargaretARABIDOPSIS THALIANACRYPTOCHROMEOXIDATIVE STRESSPHOTOMORPHOGENESISPHOTORECEPTORREACTIVE OXYGEN SPECIES (ROS) SIGNALINGhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Cryptochromes are widespread blue-light absorbing flavoproteins with important signaling roles. In plants they mediate de-etiolation, developmental and stress responses resulting from interaction with downstream signaling partners such as transcription factors and components of the proteasome. Recently, it has been shown that Arabidopsis cry1 activation by blue light also results in direct enzymatic conversion of molecular oxygen (O2) to reactive oxygen species (ROS) and hydrogen peroxide (H2O2) in vitro. Here we explored whether direct enzymatic synthesis of ROS by Arabidopsis cry1 can play a physiological role in vivo. ROS formation resulting from cry1 expression was measured by fluorescence assay in insect cell cultures and in Arabidopsis protoplasts from cryptochrome mutant seedlings. Cell death was determined by colorimetric assay. We found that ROS formation results from cry1 activation and induces cell death in insect cell cultures. In plant protoplasts, cryptochrome activation results in rapid increase in ROS formation and cell death. We conclude that ROS formation by cryptochromes may indeed be of physiological relevance and could represent a novel paradigm for cryptochrome signaling.Fil: Consentino, Laurent. Université Pierre et Marie Curie; FranciaFil: Lambert, Stefan. Université Pierre et Marie Curie; FranciaFil: Martino, Carlos. Université Pierre et Marie Curie; Francia. University of Florida; Estados UnidosFil: Jourdan, Nathalie. Université Pierre et Marie Curie; FranciaFil: Bouchet, Pierre Etienne. Université Pierre et Marie Curie; FranciaFil: Witczak, Jacques. Université Pierre et Marie Curie; FranciaFil: Castello, Pablo Raul. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Université Pierre et Marie Curie; FranciaFil: El-Esawi, Mohamed. Université Pierre et Marie Curie; Francia. Tanta University; EgiptoFil: Corbineau, Francoise. Université Pierre et Marie Curie; FranciaFil: d'Harlingue, Alain. Université Pierre et Marie Curie; FranciaFil: Ahmad, Margaret. Université Pierre et Marie Curie; Francia. Universidad Xavier; Estados UnidosWiley Blackwell Publishing, Inc2015-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/99292Consentino, Laurent; Lambert, Stefan; Martino, Carlos; Jourdan, Nathalie; Bouchet, Pierre Etienne; et al.; Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism; Wiley Blackwell Publishing, Inc; New Phytologist; 206; 4; 6-2015; 1450-14620028-646XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://nph.onlinelibrary.wiley.com/doi/full/10.1111/nph.13341info:eu-repo/semantics/altIdentifier/doi/10.1111/nph.13341info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:54:00Zoai:ri.conicet.gov.ar:11336/99292instacron: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:34982025-09-29 09:54:00.533CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism
title Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism
spellingShingle Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism
Consentino, Laurent
ARABIDOPSIS THALIANA
CRYPTOCHROME
OXIDATIVE STRESS
PHOTOMORPHOGENESIS
PHOTORECEPTOR
REACTIVE OXYGEN SPECIES (ROS) SIGNALING
title_short Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism
title_full Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism
title_fullStr Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism
title_full_unstemmed Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism
title_sort Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism
dc.creator.none.fl_str_mv Consentino, Laurent
Lambert, Stefan
Martino, Carlos
Jourdan, Nathalie
Bouchet, Pierre Etienne
Witczak, Jacques
Castello, Pablo Raul
El-Esawi, Mohamed
Corbineau, Francoise
d'Harlingue, Alain
Ahmad, Margaret
author Consentino, Laurent
author_facet Consentino, Laurent
Lambert, Stefan
Martino, Carlos
Jourdan, Nathalie
Bouchet, Pierre Etienne
Witczak, Jacques
Castello, Pablo Raul
El-Esawi, Mohamed
Corbineau, Francoise
d'Harlingue, Alain
Ahmad, Margaret
author_role author
author2 Lambert, Stefan
Martino, Carlos
Jourdan, Nathalie
Bouchet, Pierre Etienne
Witczak, Jacques
Castello, Pablo Raul
El-Esawi, Mohamed
Corbineau, Francoise
d'Harlingue, Alain
Ahmad, Margaret
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ARABIDOPSIS THALIANA
CRYPTOCHROME
OXIDATIVE STRESS
PHOTOMORPHOGENESIS
PHOTORECEPTOR
REACTIVE OXYGEN SPECIES (ROS) SIGNALING
topic ARABIDOPSIS THALIANA
CRYPTOCHROME
OXIDATIVE STRESS
PHOTOMORPHOGENESIS
PHOTORECEPTOR
REACTIVE OXYGEN SPECIES (ROS) SIGNALING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Cryptochromes are widespread blue-light absorbing flavoproteins with important signaling roles. In plants they mediate de-etiolation, developmental and stress responses resulting from interaction with downstream signaling partners such as transcription factors and components of the proteasome. Recently, it has been shown that Arabidopsis cry1 activation by blue light also results in direct enzymatic conversion of molecular oxygen (O2) to reactive oxygen species (ROS) and hydrogen peroxide (H2O2) in vitro. Here we explored whether direct enzymatic synthesis of ROS by Arabidopsis cry1 can play a physiological role in vivo. ROS formation resulting from cry1 expression was measured by fluorescence assay in insect cell cultures and in Arabidopsis protoplasts from cryptochrome mutant seedlings. Cell death was determined by colorimetric assay. We found that ROS formation results from cry1 activation and induces cell death in insect cell cultures. In plant protoplasts, cryptochrome activation results in rapid increase in ROS formation and cell death. We conclude that ROS formation by cryptochromes may indeed be of physiological relevance and could represent a novel paradigm for cryptochrome signaling.
Fil: Consentino, Laurent. Université Pierre et Marie Curie; Francia
Fil: Lambert, Stefan. Université Pierre et Marie Curie; Francia
Fil: Martino, Carlos. Université Pierre et Marie Curie; Francia. University of Florida; Estados Unidos
Fil: Jourdan, Nathalie. Université Pierre et Marie Curie; Francia
Fil: Bouchet, Pierre Etienne. Université Pierre et Marie Curie; Francia
Fil: Witczak, Jacques. Université Pierre et Marie Curie; Francia
Fil: Castello, Pablo Raul. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Université Pierre et Marie Curie; Francia
Fil: El-Esawi, Mohamed. Université Pierre et Marie Curie; Francia. Tanta University; Egipto
Fil: Corbineau, Francoise. Université Pierre et Marie Curie; Francia
Fil: d'Harlingue, Alain. Université Pierre et Marie Curie; Francia
Fil: Ahmad, Margaret. Université Pierre et Marie Curie; Francia. Universidad Xavier; Estados Unidos
description Cryptochromes are widespread blue-light absorbing flavoproteins with important signaling roles. In plants they mediate de-etiolation, developmental and stress responses resulting from interaction with downstream signaling partners such as transcription factors and components of the proteasome. Recently, it has been shown that Arabidopsis cry1 activation by blue light also results in direct enzymatic conversion of molecular oxygen (O2) to reactive oxygen species (ROS) and hydrogen peroxide (H2O2) in vitro. Here we explored whether direct enzymatic synthesis of ROS by Arabidopsis cry1 can play a physiological role in vivo. ROS formation resulting from cry1 expression was measured by fluorescence assay in insect cell cultures and in Arabidopsis protoplasts from cryptochrome mutant seedlings. Cell death was determined by colorimetric assay. We found that ROS formation results from cry1 activation and induces cell death in insect cell cultures. In plant protoplasts, cryptochrome activation results in rapid increase in ROS formation and cell death. We conclude that ROS formation by cryptochromes may indeed be of physiological relevance and could represent a novel paradigm for cryptochrome signaling.
publishDate 2015
dc.date.none.fl_str_mv 2015-06
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/11336/99292
Consentino, Laurent; Lambert, Stefan; Martino, Carlos; Jourdan, Nathalie; Bouchet, Pierre Etienne; et al.; Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism; Wiley Blackwell Publishing, Inc; New Phytologist; 206; 4; 6-2015; 1450-1462
0028-646X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/99292
identifier_str_mv Consentino, Laurent; Lambert, Stefan; Martino, Carlos; Jourdan, Nathalie; Bouchet, Pierre Etienne; et al.; Blue-light dependent reactive oxygen species formation by Arabidopsis cryptochrome may define a novel evolutionarily conserved signaling mechanism; Wiley Blackwell Publishing, Inc; New Phytologist; 206; 4; 6-2015; 1450-1462
0028-646X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://nph.onlinelibrary.wiley.com/doi/full/10.1111/nph.13341
info:eu-repo/semantics/altIdentifier/doi/10.1111/nph.13341
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 Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, 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
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