A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2

Autores
Garcia-Mata, Carlos; Wan, Jianwen; Gajdanowicz, Pawel; Gonzalez, Wendy; Hills, Adrian; Donald, Naomi; Riedelsberger, Janin; Amtmann, Anna; Dreyer, Ingo; Blatt, Michael R.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Reactive oxygen species (ROS) are essential for development and stress signalling in plants. They contribute to plant defense against pathogens, regulate stomatal transpiration and influence nutrient uptake and partitioning. Although both Ca2+ and K+ channels of plants are known to be affected, virtually nothing is known of the targets for ROS at a molecular level. Here we report that a single cysteine (Cys) residue within the Kv-like SKOR K+ channel of Arabidopsis thaliana is essential for channel sensitivity to the ROS H2O2. We show that H2O2 rapidly enhanced current amplitude and activation kinetics of heterologouslyexpressed SKOR, and the effects were reversed by the reducing agent dithiothreitol (DTT). Both H2O2 and DTT were active at the outer face of the membrane and current enhancement was strongly dependent on membrane depolarization, consistent with a H2O2-sensitive site on the SKOR protein which is exposed to the outside when the channel is in the open conformation. Cys substitutions identified a single residue, C168 located within the S3 α-helix of the voltage sensor complex, to be essential for sensitivity to H2O2. The same Cys residue was a primary determinant for current block by covalent Cys S-methioylation with aqueous methanethiosulfonates. These, and additional data identify C168 as a critical target for H2O2, and implicate ROSmediated control of the K+ channel in regulating mineral nutrient partitioning within the plant.
Fil: Garcia-Mata, Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina
Fil: Wan, Jianwen. Soochow University; China
Fil: Gajdanowicz, Pawel. Universität Potsdam; Alemania
Fil: Gonzalez, Wendy. Universidad de Talca; Chile
Fil: Hills, Adrian.
Fil: Donald, Naomi.
Fil: Riedelsberger, Janin.
Fil: Amtmann, Anna. Universität Potsdam; Alemania
Fil: Dreyer, Ingo. Universität Potsdam; Alemania
Fil: Blatt, Michael R..
Materia
SKOR K+ channel
Reactive Oxygen Species
H2O2
Cysteine Modification
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:11336/14438
Acceder
id CONICETDig_5448108e51dd4418dd4d6b152c895244
oai_identifier_str oai:ri.conicet.gov.ar:11336/14438
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2Garcia-Mata, CarlosWan, JianwenGajdanowicz, PawelGonzalez, WendyHills, AdrianDonald, NaomiRiedelsberger, JaninAmtmann, AnnaDreyer, IngoBlatt, Michael R.SKOR K+ channelReactive Oxygen SpeciesH2O2Cysteine Modificationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Reactive oxygen species (ROS) are essential for development and stress signalling in plants. They contribute to plant defense against pathogens, regulate stomatal transpiration and influence nutrient uptake and partitioning. Although both Ca2+ and K+ channels of plants are known to be affected, virtually nothing is known of the targets for ROS at a molecular level. Here we report that a single cysteine (Cys) residue within the Kv-like SKOR K+ channel of Arabidopsis thaliana is essential for channel sensitivity to the ROS H2O2. We show that H2O2 rapidly enhanced current amplitude and activation kinetics of heterologouslyexpressed SKOR, and the effects were reversed by the reducing agent dithiothreitol (DTT). Both H2O2 and DTT were active at the outer face of the membrane and current enhancement was strongly dependent on membrane depolarization, consistent with a H2O2-sensitive site on the SKOR protein which is exposed to the outside when the channel is in the open conformation. Cys substitutions identified a single residue, C168 located within the S3 α-helix of the voltage sensor complex, to be essential for sensitivity to H2O2. The same Cys residue was a primary determinant for current block by covalent Cys S-methioylation with aqueous methanethiosulfonates. These, and additional data identify C168 as a critical target for H2O2, and implicate ROSmediated control of the K+ channel in regulating mineral nutrient partitioning within the plant.Fil: Garcia-Mata, Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; ArgentinaFil: Wan, Jianwen. Soochow University; ChinaFil: Gajdanowicz, Pawel. Universität Potsdam; AlemaniaFil: Gonzalez, Wendy. Universidad de Talca; ChileFil: Hills, Adrian.Fil: Donald, Naomi.Fil: Riedelsberger, Janin.Fil: Amtmann, Anna. Universität Potsdam; AlemaniaFil: Dreyer, Ingo. Universität Potsdam; AlemaniaFil: Blatt, Michael R..American Society For Biochemistry And Molecular Biology2010-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/14438Garcia-Mata, Carlos; Wan, Jianwen; Gajdanowicz, Pawel; Gonzalez, Wendy; Hills, Adrian; et al.; A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 285; 7-2010; 29286-292940021-9258enginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/285/38/29286.abstract?sid=b4ffdf4d-fc17-4326-be88-267c5036d891info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M110.141176info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:22:01Zoai:ri.conicet.gov.ar:11336/14438instacron: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 10:22:01.315CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2
title A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2
spellingShingle A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2
Garcia-Mata, Carlos
SKOR K+ channel
Reactive Oxygen Species
H2O2
Cysteine Modification
title_short A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2
title_full A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2
title_fullStr A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2
title_full_unstemmed A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2
title_sort A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2
dc.creator.none.fl_str_mv Garcia-Mata, Carlos
Wan, Jianwen
Gajdanowicz, Pawel
Gonzalez, Wendy
Hills, Adrian
Donald, Naomi
Riedelsberger, Janin
Amtmann, Anna
Dreyer, Ingo
Blatt, Michael R.
author Garcia-Mata, Carlos
author_facet Garcia-Mata, Carlos
Wan, Jianwen
Gajdanowicz, Pawel
Gonzalez, Wendy
Hills, Adrian
Donald, Naomi
Riedelsberger, Janin
Amtmann, Anna
Dreyer, Ingo
Blatt, Michael R.
author_role author
author2 Wan, Jianwen
Gajdanowicz, Pawel
Gonzalez, Wendy
Hills, Adrian
Donald, Naomi
Riedelsberger, Janin
Amtmann, Anna
Dreyer, Ingo
Blatt, Michael R.
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv SKOR K+ channel
Reactive Oxygen Species
H2O2
Cysteine Modification
topic SKOR K+ channel
Reactive Oxygen Species
H2O2
Cysteine Modification
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Reactive oxygen species (ROS) are essential for development and stress signalling in plants. They contribute to plant defense against pathogens, regulate stomatal transpiration and influence nutrient uptake and partitioning. Although both Ca2+ and K+ channels of plants are known to be affected, virtually nothing is known of the targets for ROS at a molecular level. Here we report that a single cysteine (Cys) residue within the Kv-like SKOR K+ channel of Arabidopsis thaliana is essential for channel sensitivity to the ROS H2O2. We show that H2O2 rapidly enhanced current amplitude and activation kinetics of heterologouslyexpressed SKOR, and the effects were reversed by the reducing agent dithiothreitol (DTT). Both H2O2 and DTT were active at the outer face of the membrane and current enhancement was strongly dependent on membrane depolarization, consistent with a H2O2-sensitive site on the SKOR protein which is exposed to the outside when the channel is in the open conformation. Cys substitutions identified a single residue, C168 located within the S3 α-helix of the voltage sensor complex, to be essential for sensitivity to H2O2. The same Cys residue was a primary determinant for current block by covalent Cys S-methioylation with aqueous methanethiosulfonates. These, and additional data identify C168 as a critical target for H2O2, and implicate ROSmediated control of the K+ channel in regulating mineral nutrient partitioning within the plant.
Fil: Garcia-Mata, Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina
Fil: Wan, Jianwen. Soochow University; China
Fil: Gajdanowicz, Pawel. Universität Potsdam; Alemania
Fil: Gonzalez, Wendy. Universidad de Talca; Chile
Fil: Hills, Adrian.
Fil: Donald, Naomi.
Fil: Riedelsberger, Janin.
Fil: Amtmann, Anna. Universität Potsdam; Alemania
Fil: Dreyer, Ingo. Universität Potsdam; Alemania
Fil: Blatt, Michael R..
description Reactive oxygen species (ROS) are essential for development and stress signalling in plants. They contribute to plant defense against pathogens, regulate stomatal transpiration and influence nutrient uptake and partitioning. Although both Ca2+ and K+ channels of plants are known to be affected, virtually nothing is known of the targets for ROS at a molecular level. Here we report that a single cysteine (Cys) residue within the Kv-like SKOR K+ channel of Arabidopsis thaliana is essential for channel sensitivity to the ROS H2O2. We show that H2O2 rapidly enhanced current amplitude and activation kinetics of heterologouslyexpressed SKOR, and the effects were reversed by the reducing agent dithiothreitol (DTT). Both H2O2 and DTT were active at the outer face of the membrane and current enhancement was strongly dependent on membrane depolarization, consistent with a H2O2-sensitive site on the SKOR protein which is exposed to the outside when the channel is in the open conformation. Cys substitutions identified a single residue, C168 located within the S3 α-helix of the voltage sensor complex, to be essential for sensitivity to H2O2. The same Cys residue was a primary determinant for current block by covalent Cys S-methioylation with aqueous methanethiosulfonates. These, and additional data identify C168 as a critical target for H2O2, and implicate ROSmediated control of the K+ channel in regulating mineral nutrient partitioning within the plant.
publishDate 2010
dc.date.none.fl_str_mv 2010-07
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/11336/14438
Garcia-Mata, Carlos; Wan, Jianwen; Gajdanowicz, Pawel; Gonzalez, Wendy; Hills, Adrian; et al.; A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 285; 7-2010; 29286-29294
0021-9258
url http://hdl.handle.net/11336/14438
identifier_str_mv Garcia-Mata, Carlos; Wan, Jianwen; Gajdanowicz, Pawel; Gonzalez, Wendy; Hills, Adrian; et al.; A Minimal Cysteine Motif Required To Activate The SKOR K+ Channel Of Arabidopsis By The Reactive Oxygen Species H2O2; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 285; 7-2010; 29286-29294
0021-9258
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/285/38/29286.abstract?sid=b4ffdf4d-fc17-4326-be88-267c5036d891
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M110.141176
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 Society For Biochemistry And Molecular Biology
publisher.none.fl_str_mv American Society For Biochemistry And Molecular Biology
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 13.070432

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