The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit

Autores
Lascano, Hernan Ramiro; Casano, Leonardo M.; Martı́n, Mercedes; Sabater, Bartolomé
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Hydrogen peroxide (H2O2) induces increases, to different degrees, in transcripts, protein levels, and activity of the Ndh complex (EC 1.6.5.3). In the present work, we have compared the effects of relatively excess light, H2O2, dimethylthiourea (a scavenger of H2O2), and/or EGTA (a Ca2+chelator) on the activity and protein levels of the Ndh complex of barley (Hordeum vulgare cv Hassan) leaf segments. The results show the involvement of H2O2 in the modulation of both the protein level and activity of the Ndh complex and the participation of Ca2+ mainly in the activity regulation of pre-existing protein. Changes in Ndh complex activity could not be explained only by changes in Ndh protein levels, suggesting posttranslational modifications. Hence, we investigate the possible phosphorylation of the Ndh complex both in thylakoids and in the immunopurified Ndh complex using monoclonal phosphoamino acid antibodies. We demonstrate that the Ndh complex is phosphorylated in vivo at threonine residue(s) of the NDH-F polypeptide and that the level of phosphorylation is closely correlated with the Ndh complex activity. The emerging picture is that full activity of the Ndh complex is reached by phosphorylation of its NDH-F subunit in a H2O2- and Ca2+-mediated action.
Instituto de Fisiología y Recursos Genéticos Vegetales
Fil: Lascano, Hernán Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lascano, Hernán Ramiro. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Fisiología y Recursos Genéticos Vegetales. Argentina
Fil: Lascano, Hernán Ramiro. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; España
Fil: Casano, Leonardo M. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; España
Fil: Martín, Mercedes. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; España
Fil: Sabater, Bartolomé. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; España
Fuente
Plant Physiology 132 (1) : 256-262 (May 2003)
Materia
Hydrogen Peroxide
Peróxido de Hidrógeno
Fosforilación
Phosphorylation
Agua Oxigenada
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/10935
Acceder
id INTADig_e3a56f4c436d883ec36557a5729b5748
oai_identifier_str oai:localhost:20.500.12123/10935
network_acronym_str INTADig
repository_id_str l
network_name_str INTA Digital (INTA)
spelling The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F SubunitLascano, Hernan RamiroCasano, Leonardo M.Martı́n, MercedesSabater, BartoloméHydrogen PeroxidePeróxido de HidrógenoFosforilaciónPhosphorylationAgua OxigenadaHydrogen peroxide (H2O2) induces increases, to different degrees, in transcripts, protein levels, and activity of the Ndh complex (EC 1.6.5.3). In the present work, we have compared the effects of relatively excess light, H2O2, dimethylthiourea (a scavenger of H2O2), and/or EGTA (a Ca2+chelator) on the activity and protein levels of the Ndh complex of barley (Hordeum vulgare cv Hassan) leaf segments. The results show the involvement of H2O2 in the modulation of both the protein level and activity of the Ndh complex and the participation of Ca2+ mainly in the activity regulation of pre-existing protein. Changes in Ndh complex activity could not be explained only by changes in Ndh protein levels, suggesting posttranslational modifications. Hence, we investigate the possible phosphorylation of the Ndh complex both in thylakoids and in the immunopurified Ndh complex using monoclonal phosphoamino acid antibodies. We demonstrate that the Ndh complex is phosphorylated in vivo at threonine residue(s) of the NDH-F polypeptide and that the level of phosphorylation is closely correlated with the Ndh complex activity. The emerging picture is that full activity of the Ndh complex is reached by phosphorylation of its NDH-F subunit in a H2O2- and Ca2+-mediated action.Instituto de Fisiología y Recursos Genéticos VegetalesFil: Lascano, Hernán Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Lascano, Hernán Ramiro. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Fisiología y Recursos Genéticos Vegetales. ArgentinaFil: Lascano, Hernán Ramiro. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; EspañaFil: Casano, Leonardo M. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; EspañaFil: Martín, Mercedes. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; EspañaFil: Sabater, Bartolomé. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; EspañaAmerican Society of Plant Biologists2021-12-17T19:49:34Z2021-12-17T19:49:34Z2003-05-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/10935https://academic.oup.com/plphys/article/132/1/256/61118310032-08891532-2548 (online)https://doi.org/10.1104/pp.103.020321Plant Physiology 132 (1) : 256-262 (May 2003)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-09-29T13:45:25Zoai:localhost:20.500.12123/10935instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-09-29 13:45:26.294INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit
title The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit
spellingShingle The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit
Lascano, Hernan Ramiro
Hydrogen Peroxide
Peróxido de Hidrógeno
Fosforilación
Phosphorylation
Agua Oxigenada
title_short The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit
title_full The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit
title_fullStr The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit
title_full_unstemmed The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit
title_sort The Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunit
dc.creator.none.fl_str_mv Lascano, Hernan Ramiro
Casano, Leonardo M.
Martı́n, Mercedes
Sabater, Bartolomé
author Lascano, Hernan Ramiro
author_facet Lascano, Hernan Ramiro
Casano, Leonardo M.
Martı́n, Mercedes
Sabater, Bartolomé
author_role author
author2 Casano, Leonardo M.
Martı́n, Mercedes
Sabater, Bartolomé
author2_role author
author
author
dc.subject.none.fl_str_mv Hydrogen Peroxide
Peróxido de Hidrógeno
Fosforilación
Phosphorylation
Agua Oxigenada
topic Hydrogen Peroxide
Peróxido de Hidrógeno
Fosforilación
Phosphorylation
Agua Oxigenada
dc.description.none.fl_txt_mv Hydrogen peroxide (H2O2) induces increases, to different degrees, in transcripts, protein levels, and activity of the Ndh complex (EC 1.6.5.3). In the present work, we have compared the effects of relatively excess light, H2O2, dimethylthiourea (a scavenger of H2O2), and/or EGTA (a Ca2+chelator) on the activity and protein levels of the Ndh complex of barley (Hordeum vulgare cv Hassan) leaf segments. The results show the involvement of H2O2 in the modulation of both the protein level and activity of the Ndh complex and the participation of Ca2+ mainly in the activity regulation of pre-existing protein. Changes in Ndh complex activity could not be explained only by changes in Ndh protein levels, suggesting posttranslational modifications. Hence, we investigate the possible phosphorylation of the Ndh complex both in thylakoids and in the immunopurified Ndh complex using monoclonal phosphoamino acid antibodies. We demonstrate that the Ndh complex is phosphorylated in vivo at threonine residue(s) of the NDH-F polypeptide and that the level of phosphorylation is closely correlated with the Ndh complex activity. The emerging picture is that full activity of the Ndh complex is reached by phosphorylation of its NDH-F subunit in a H2O2- and Ca2+-mediated action.
Instituto de Fisiología y Recursos Genéticos Vegetales
Fil: Lascano, Hernán Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Lascano, Hernán Ramiro. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Fisiología y Recursos Genéticos Vegetales. Argentina
Fil: Lascano, Hernán Ramiro. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; España
Fil: Casano, Leonardo M. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; España
Fil: Martín, Mercedes. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; España
Fil: Sabater, Bartolomé. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; España
description Hydrogen peroxide (H2O2) induces increases, to different degrees, in transcripts, protein levels, and activity of the Ndh complex (EC 1.6.5.3). In the present work, we have compared the effects of relatively excess light, H2O2, dimethylthiourea (a scavenger of H2O2), and/or EGTA (a Ca2+chelator) on the activity and protein levels of the Ndh complex of barley (Hordeum vulgare cv Hassan) leaf segments. The results show the involvement of H2O2 in the modulation of both the protein level and activity of the Ndh complex and the participation of Ca2+ mainly in the activity regulation of pre-existing protein. Changes in Ndh complex activity could not be explained only by changes in Ndh protein levels, suggesting posttranslational modifications. Hence, we investigate the possible phosphorylation of the Ndh complex both in thylakoids and in the immunopurified Ndh complex using monoclonal phosphoamino acid antibodies. We demonstrate that the Ndh complex is phosphorylated in vivo at threonine residue(s) of the NDH-F polypeptide and that the level of phosphorylation is closely correlated with the Ndh complex activity. The emerging picture is that full activity of the Ndh complex is reached by phosphorylation of its NDH-F subunit in a H2O2- and Ca2+-mediated action.
publishDate 2003
dc.date.none.fl_str_mv 2003-05-01
2021-12-17T19:49:34Z
2021-12-17T19:49:34Z
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/20.500.12123/10935
https://academic.oup.com/plphys/article/132/1/256/6111831
0032-0889
1532-2548 (online)
https://doi.org/10.1104/pp.103.020321
url http://hdl.handle.net/20.500.12123/10935
https://academic.oup.com/plphys/article/132/1/256/6111831
https://doi.org/10.1104/pp.103.020321
identifier_str_mv 0032-0889
1532-2548 (online)
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Society of Plant Biologists
publisher.none.fl_str_mv American Society of Plant Biologists
dc.source.none.fl_str_mv Plant Physiology 132 (1) : 256-262 (May 2003)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
_version_ 1844619160593629184
score 12.559606

Publicaciones similares