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Abstract
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 [ver mas...]
dc.contributor.authorLascano, Hernan Ramiro
dc.contributor.authorCasano, Leonardo M.
dc.contributor.authorMartı́n, Mercedes
dc.contributor.authorSabater, Bartolomé
dc.date.accessioned2021-12-17T19:49:34Z
dc.date.available2021-12-17T19:49:34Z
dc.date.issued2003-05-01
dc.identifier.issn0032-0889
dc.identifier.issn1532-2548 (online)
dc.identifier.otherhttps://doi.org/10.1104/pp.103.020321
dc.identifier.urihttp://hdl.handle.net/20.500.12123/10935
dc.identifier.urihttps://academic.oup.com/plphys/article/132/1/256/6111831
dc.description.abstractHydrogen 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.eng
dc.formatapplication/pdfes_AR
dc.language.isoenges_AR
dc.publisherAmerican Society of Plant Biologistses_AR
dc.rightsinfo:eu-repo/semantics/openAccesses_AR
dc.sourcePlant Physiology 132 (1) : 256-262 (May 2003)es_AR
dc.subjectHydrogen Peroxidees_AR
dc.subjectPeróxido de Hidrógeno
dc.subjectFosforilación
dc.subjectPhosphorylationeng
dc.subject.otherAgua Oxigenada
dc.titleThe Activity of the Chloroplastic Ndh Complex Is Regulated by Phosphorylation of the NDH-F Subunites_AR
dc.typeinfo:ar-repo/semantics/artículoes_AR
dc.typeinfo:eu-repo/semantics/articlees_AR
dc.typeinfo:eu-repo/semantics/publishedVersiones_AR
dc.description.origenInstituto de Fisiología y Recursos Genéticos Vegetaleses_AR
dc.description.filFil: Lascano, Hernán Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentinaes_AR
dc.description.filFil: Lascano, Hernán Ramiro. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Fisiología y Recursos Genéticos Vegetales. Argentinaes_AR
dc.description.filFil: Lascano, Hernán Ramiro. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; Españaes_AR
dc.description.filFil: Casano, Leonardo M. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; Españaes_AR
dc.description.filFil: Martín, Mercedes. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; Españaes_AR
dc.description.filFil: Sabater, Bartolomé. Universidad de Alcalá de Henares. Departamento de Biología Vegetal; Españaes_AR
dc.subtypecientifico


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