中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7

文献类型:期刊论文

作者Wu, Jianghao2; Rong, Liwei2; Lin, Weijun2; Kong, Lingxi2; Wei, Dengjie2; Zhang, Lixin; Rochaix, Jean-David; Xu, Xiumei3
刊名PLANT PHYSIOLOGY
出版日期2021
卷号186期号:2页码:964-976
ISSN号0032-0889
DOI10.1093/plphys/kiab091
文献子类Article
英文摘要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.
学科主题Plant Sciences
出版地CARY
电子版国际标准刊号1532-2548
WOS关键词CYTOCHROME B(6)F COMPLEX ; STATE TRANSITIONS ; REDUCING EQUIVALENTS ; THYLAKOID MEMBRANE ; PHOTOSYSTEM-II ; SUBUNIT-IV ; PHOSPHORYLATION ; THIOREDOXIN ; IDENTIFICATION ; LTO1/ATVKOR
WOS研究方向Science Citation Index Expanded (SCI-EXPANDED)
语种英语
WOS记录号WOS:000671555900021
出版者OXFORD UNIV PRESS INC
资助机构National Key Research and Development Program [2020YFA0907600] ; National Natural Science Foundation of China [31700204, 31661143026] ; 111 Project [D16014] ; Outstanding Talents Fund of Henan University, China
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/26523]  
专题中科院光生物学重点实验室
作者单位1.Univ Geneva, Dept Mol Biol, CH-1211 Geneva, Switzerland
2.Chinese Acad Sci, Photosynth Res Ctr, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Henan Univ, Sch Life Sci, State Key Lab Crop Stress Adaptat & Improvement, Jinming Ave, Kaifeng 475004, Peoples R China
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GB/T 7714
Wu, Jianghao,Rong, Liwei,Lin, Weijun,et al. Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7[J]. PLANT PHYSIOLOGY,2021,186(2):964-976.
APA Wu, Jianghao.,Rong, Liwei.,Lin, Weijun.,Kong, Lingxi.,Wei, Dengjie.,...&Xu, Xiumei.(2021).Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7.PLANT PHYSIOLOGY,186(2),964-976.
MLA Wu, Jianghao,et al."Functional redox links between lumen thiol oxidoreductase1 and serine/threonine-protein kinase STN7".PLANT PHYSIOLOGY 186.2(2021):964-976.

入库方式: OAI收割

来源:植物研究所

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