Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7
In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and mitigates photo-damage. The serine/threonine-protein kinase STN7 phosphorylates the light-harvesting complex of photosystem II (PSII; light-harve...
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Published in | Plant physiology (Bethesda) Vol. 186; no. 2; pp. 964 - 976 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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Oxford University Press
11.06.2021
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Abstract | In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and mitigates photo-damage. The serine/threonine-protein kinase STN7 phosphorylates the light-harvesting complex of photosystem II (PSII; light-harvesting complex II), which then migrates from PSII to photosystem I (PSI), thereby rebalancing the light excitation energy between the photosystems and restoring the redox poise of the photosynthetic electron transport chain. Two conserved cysteines forming intra- or intermolecular disulfide bonds in the lumenal domain (LD) of STN7 are essential for the kinase activity although it is still unknown how activation of the kinase is regulated. In this study, we show lumen thiol oxidoreductase 1 (LTO1) is co-expressed with STN7 in Arabidopsis (Arabidopsis thaliana) and interacts with the LD of STN7 in vitro and in vivo. LTO1 contains thioredoxin (TRX)-like and vitamin K epoxide reductase domains which are related to the disulfide-bond formation system in bacteria. We further show that the TRX-like domain of LTO1 is able to oxidize the conserved lumenal cysteines of STN7 in vitro. In addition, loss of LTO1 affects the kinase activity of STN7 in Arabidopsis. Based on these results, we propose that LTO1 helps to maintain STN7 in an oxidized active state in state 2 through redox interactions between the lumenal cysteines of STN7 and LTO1. |
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AbstractList | LTO1 maintains the active oxidized redox state of the STN7 protein kinase on the thylakoid lumen side during state transitions.
In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and mitigates photo-damage. The serine/threonine-protein kinase STN7 phosphorylates the light-harvesting complex of photosystem II (PSII; light-harvesting complex II), which then migrates from PSII to photosystem I (PSI), thereby rebalancing the light excitation energy between the photosystems and restoring the redox poise of the photosynthetic electron transport chain. Two conserved cysteines forming intra- or intermolecular disulfide bonds in the lumenal domain (LD) of STN7 are essential for the kinase activity although it is still unknown how activation of the kinase is regulated. In this study, we show lumen thiol oxidoreductase 1 (LTO1) is co-expressed with STN7 in Arabidopsis (
Arabidopsis thaliana
) and interacts with the LD of STN7 in vitro and in vivo. LTO1 contains thioredoxin (TRX)-like and vitamin K epoxide reductase domains which are related to the disulfide-bond formation system in bacteria. We further show that the TRX-like domain of LTO1 is able to oxidize the conserved lumenal cysteines of STN7 in vitro. In addition, loss of LTO1 affects the kinase activity of STN7 in Arabidopsis. Based on these results, we propose that LTO1 helps to maintain STN7 in an oxidized active state in state 2 through redox interactions between the lumenal cysteines of STN7 and LTO1. In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and mitigates photo-damage. The serine/threonine-protein kinase STN7 phosphorylates the light-harvesting complex of photosystem II (PSII; light-harvesting complex II), which then migrates from PSII to photosystem I (PSI), thereby rebalancing the light excitation energy between the photosystems and restoring the redox poise of the photosynthetic electron transport chain. Two conserved cysteines forming intra- or intermolecular disulfide bonds in the lumenal domain (LD) of STN7 are essential for the kinase activity although it is still unknown how activation of the kinase is regulated. In this study, we show lumen thiol oxidoreductase 1 (LTO1) is co-expressed with STN7 in Arabidopsis (Arabidopsis thaliana) and interacts with the LD of STN7 in vitro and in vivo. LTO1 contains thioredoxin (TRX)-like and vitamin K epoxide reductase domains which are related to the disulfide-bond formation system in bacteria. We further show that the TRX-like domain of LTO1 is able to oxidize the conserved lumenal cysteines of STN7 in vitro. In addition, loss of LTO1 affects the kinase activity of STN7 in Arabidopsis. Based on these results, we propose that LTO1 helps to maintain STN7 in an oxidized active state in state 2 through redox interactions between the lumenal cysteines of STN7 and LTO1. Abstract In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and mitigates photo-damage. The serine/threonine-protein kinase STN7 phosphorylates the light-harvesting complex of photosystem II (PSII; light-harvesting complex II), which then migrates from PSII to photosystem I (PSI), thereby rebalancing the light excitation energy between the photosystems and restoring the redox poise of the photosynthetic electron transport chain. Two conserved cysteines forming intra- or intermolecular disulfide bonds in the lumenal domain (LD) of STN7 are essential for the kinase activity although it is still unknown how activation of the kinase is regulated. In this study, we show lumen thiol oxidoreductase 1 (LTO1) is co-expressed with STN7 in Arabidopsis (Arabidopsis thaliana) and interacts with the LD of STN7 in vitro and in vivo. LTO1 contains thioredoxin (TRX)-like and vitamin K epoxide reductase domains which are related to the disulfide-bond formation system in bacteria. We further show that the TRX-like domain of LTO1 is able to oxidize the conserved lumenal cysteines of STN7 in vitro. In addition, loss of LTO1 affects the kinase activity of STN7 in Arabidopsis. Based on these results, we propose that LTO1 helps to maintain STN7 in an oxidized active state in state 2 through redox interactions between the lumenal cysteines of STN7 and LTO1. |
Author | Lin, Weijun Wu, Jianghao Rong, Liwei Xu, Xiumei Kong, Lingxi Wei, Dengjie Rochaix, Jean-David Zhang, Lixin |
AuthorAffiliation | 1 Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences , Beijing 100093, China 5 Department of Plant Biology, University of Geneva , Geneva 1211, Switzerland 2 University of Chinese Academy of Sciences , Beijing 100049, China 3 State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University , Kaifeng 475004, China 4 Department of Molecular Biology, University of Geneva , Geneva 1211, Switzerland |
AuthorAffiliation_xml | – name: 4 Department of Molecular Biology, University of Geneva , Geneva 1211, Switzerland – name: 1 Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences , Beijing 100093, China – name: 2 University of Chinese Academy of Sciences , Beijing 100049, China – name: 5 Department of Plant Biology, University of Geneva , Geneva 1211, Switzerland – name: 3 State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University , Kaifeng 475004, China |
Author_xml | – sequence: 1 givenname: Jianghao surname: Wu fullname: Wu, Jianghao organization: University of Chinese Academy of Sciences, Beijing 100049, China – sequence: 2 givenname: Liwei surname: Rong fullname: Rong, Liwei organization: University of Chinese Academy of Sciences, Beijing 100049, China – sequence: 3 givenname: Weijun surname: Lin fullname: Lin, Weijun organization: University of Chinese Academy of Sciences, Beijing 100049, China – sequence: 4 givenname: Lingxi surname: Kong fullname: Kong, Lingxi organization: University of Chinese Academy of Sciences, Beijing 100049, China – sequence: 5 givenname: Dengjie surname: Wei fullname: Wei, Dengjie organization: University of Chinese Academy of Sciences, Beijing 100049, China – sequence: 6 givenname: Lixin surname: Zhang fullname: Zhang, Lixin organization: State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng 475004, China – sequence: 7 givenname: Jean-David orcidid: 0000-0001-8483-777X surname: Rochaix fullname: Rochaix, Jean-David organization: Department of Plant Biology, University of Geneva, Geneva 1211, Switzerland – sequence: 8 givenname: Xiumei orcidid: 0000-0003-3515-1864 surname: Xu fullname: Xu, Xiumei organization: State Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, Kaifeng 475004, China |
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Snippet | In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield and... Abstract In response to changing light quantity and quality, photosynthetic organisms perform state transitions, a process which optimizes photosynthetic yield... LTO1 maintains the active oxidized redox state of the STN7 protein kinase on the thylakoid lumen side during state transitions. In response to changing light... |
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SubjectTerms | Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis - physiology Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Oxidation-Reduction Phosphorylation Photosynthesis Photosystem I Protein Complex - metabolism Photosystem II Protein Complex - metabolism Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - metabolism Sulfhydryl Compounds - metabolism Vitamin K Epoxide Reductases - genetics Vitamin K Epoxide Reductases - metabolism |
Title | Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7 |
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