Overexpression of thioredoxin m in tobacco chloroplasts inhibits the protein kinase STN7 and alters photosynthetic performance

Ancín Rípodas, María; Fernández San Millán, Alicia; Larraya Reta, Luis María; Morales Iribas, Fermín; Veramendi Charola, Jon; Aranjuelo Michelena, Iker; Farrán Blanch, Inmaculada

Overexpression of thioredoxin m in tobacco chloroplasts inhibits the protein kinase STN7 and alters photosynthetic performance

dc.contributor.author	Ancín Rípodas, María
dc.contributor.author	Fernández San Millán, Alicia
dc.contributor.author	Larraya Reta, Luis María
dc.contributor.author	Morales Iribas, Fermín
dc.contributor.author	Veramendi Charola, Jon
dc.contributor.author	Aranjuelo Michelena, Iker
dc.contributor.author	Farrán Blanch, Inmaculada
dc.contributor.department	IdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutua	es_ES
dc.date.accessioned	2019-03-06T12:39:08Z
dc.date.available	2019-03-06T12:39:08Z
dc.date.issued	2019
dc.description.abstract	The 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.sponsorship	This 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.extent	12 p.
dc.format.mimetype	application/pdf	en
dc.format.mimetype	application/zip	en
dc.identifier.doi	10.1093/jxb/ery415
dc.identifier.issn	0022-0957 (Print)
dc.identifier.issn	1460-2431 (Electronic)
dc.identifier.uri	https://academica-e.unavarra.es/handle/2454/32507
dc.language.iso	eng	en
dc.publisher	Oxford University Press	en
dc.relation.ispartof	Journal of Experimental Botany, Vol. 70, No. 3 pp. 1005–1016, 2019	en
dc.relation.projectID	info:eu-repo/grantAgreement/ES/1PE/AGL2016-79868/
dc.relation.publisherversion	https://doi.org/10.1093/jxb/ery415
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.accessRights	info:eu-repo/semantics/openAccess
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/
dc.subject	LHCII phosphorylation	en
dc.subject	Nicotiana tabacum	en
dc.subject	Photosynthesis	en
dc.subject	Protein complex	en
dc.subject	Thioredoxin	en
dc.subject	Thylakoid membrane	en
dc.title	Overexpression of thioredoxin m in tobacco chloroplasts inhibits the protein kinase STN7 and alters photosynthetic performance	en
dc.type	info:eu-repo/semantics/article
dc.type.version	info:eu-repo/semantics/publishedVersion
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