Back to Search
Start Over
Overexpression of thioredoxin m in tobacco chloroplasts inhibits the protein kinase STN7 and alters photosynthetic performance
- Source :
- Journal of Experimental Botany, Digital.CSIC. Repositorio Institucional del CSIC, instname, Academica-e. Repositorio Institucional de la Universidad Pública de Navarra, Academica-e: Repositorio Institucional de la Universidad Pública de Navarra, Universidad Pública de Navarra
- Publication Year :
- 2018
-
Abstract
- 12 Pags.- 2 Tabls.- 6 Figs. © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.<br />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.<br />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).
- Subjects :
- 0106 biological sciences
0301 basic medicine
animal structures
Chloroplasts
Physiology
Plastoquinone
Plant Science
Protein Serine-Threonine Kinases
01 natural sciences
03 medical and health sciences
chemistry.chemical_compound
Chloroplast Thioredoxins
Gene Expression Regulation, Plant
Tobacco
Protein kinase A
Plant Proteins
photosynthesis
biology
Chemistry
Nicotiana tabacum
protein complex
RuBisCO
Wild type
food and beverages
Photosystem II Protein Complex
thioredoxin
thylakoid membrane
Research Papers
Cell biology
LHCII phosphorylation
Chloroplast
030104 developmental biology
Thylakoid
biology.protein
Phosphorylation
Thioredoxin
Oxidation-Reduction
010606 plant biology & botany
Photosynthesis and Metabolism
Subjects
Details
- ISSN :
- 14602431
- Volume :
- 70
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Journal of experimental botany
- Accession number :
- edsair.doi.dedup.....c2bbcb5d4507be1e8aa872bda19121ec