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dc.creatorAncín Rípodas, Maríaes_ES
dc.creatorFernández San Millán, Aliciaes_ES
dc.creatorLarraya Reta, Luis Maríaes_ES
dc.creatorMorales Iribas, Fermínes_ES
dc.creatorVeramendi Charola, Jones_ES
dc.creatorAranjuelo Michelena, Ikeres_ES
dc.creatorFarrán Blanch, Inmaculadaes_ES
dc.date.accessioned2019-03-06T12:39:08Z
dc.date.available2019-03-06T12:39:08Z
dc.date.issued2019
dc.identifier.issn0022-0957 (Print)
dc.identifier.issn1460-2431 (Electronic)
dc.identifier.urihttps://hdl.handle.net/2454/32507
dc.description.abstractThe activity of the protein kinase STN7, involved in phosphorylation of the light-harvesting complex II (LHCII) proteins, has been reported as being co-operatively regulated by the redox state of the plastoquinone pool and the ferredoxin–thioredoxin (Trx) system. The present study aims to investigate the role of plastid Trxs in STN7 regulation and their impact on photosynthesis. For this purpose, tobacco plants overexpressing Trx f or m from the plastid genome were characterized, demonstrating that only Trx m overexpression was associated with a complete loss of LHCII phosphorylation that did not correlate with decreased STN7 levels. The absence of phosphorylation in Trx m-overexpressing plants impeded migration of LHCII from PSII to PSI, with the concomitant loss of PSI–LHCII complex formation. Consequently, the thylakoid ultrastructure was altered, showing reduced grana stacking. Moreover, the electron transport rate was negatively affected, showing an impact on energy-demanding processes such as the Rubisco maximum carboxylation capacity and ribulose 1,5-bisphosphate regeneration rate values, which caused a strong depletion in net photosynthetic rates. Finally, tobacco plants overexpressing a Trx m mutant lacking the reactive redox site showed equivalent physiological performance to the wild type, indicating that the overexpressed Trx m deactivates STN7 in a redox-dependent way.en
dc.description.sponsorshipThis work was supported by the Spanish Ministry of Science and Innovation (AGL2016-79868) and from the Basque Government (UPV/EHU-GV IT-932-16). MA is a holder of a PhD fellowship from the Spanish Ministry of Education (FPU13/01675).en
dc.format.extent12 p.
dc.format.mimetypeapplication/pdfen
dc.format.mimetypeapplication/zipen
dc.language.isoengen
dc.publisherOxford University Pressen
dc.relation.ispartofJournal of Experimental Botany, Vol. 70, No. 3 pp. 1005–1016, 2019en
dc.rights© The Author(s) 2018. This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectLHCII phosphorylationen
dc.subjectNicotiana tabacumen
dc.subjectPhotosynthesisen
dc.subjectProtein complexen
dc.subjectThioredoxinen
dc.subjectThylakoid membraneen
dc.titleOverexpression of thioredoxin m in tobacco chloroplasts inhibits the protein kinase STN7 and alters photosynthetic performanceen
dc.typeArtículo / Artikuluaes
dc.typeinfo:eu-repo/semantics/articleen
dc.contributor.departmentIdAB – Instituto de Agrobiotecnología / Agrobioteknologiako Institutuaes
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.identifier.doi10.1093/jxb/ery415
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/1PE/AGL2016-79868en
dc.relation.publisherversionhttps://doi.org/10.1093/jxb/ery415
dc.type.versionVersión publicada / Argitaratu den bertsioaes
dc.type.versioninfo:eu-repo/semantics/publishedVersionen


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© The Author(s) 2018. This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
Except where otherwise noted, this item's license is described as © The Author(s) 2018. This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.