中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
OHP1, OHP2, and HCF244 Form a Transient Functional Complex with the Photosystem II Reaction Center

文献类型:期刊论文

作者Li, Yonghong2; Liu, Bei2; Zhang, Jiao; Kong, Fanna; Zhang, Lin3; Meng, Han3; Li, Wenjing4; Rochaix, Jean-David; Li, Dan; Peng, Lianwei3
刊名PLANT PHYSIOLOGY
出版日期2019
卷号179期号:1页码:195-208
ISSN号0032-0889
DOI10.1104/pp.18.01231
文献子类Article
英文摘要The reaction center (RC) of photosystem II (PSII), which is composed of D1, D2, PsbI, and cytochrome b559 subunits, forms at an early stage of PSII biogenesis. However, it is largely unclear how these components assemble to form a functional unit. In this work, we show that synthesis of the PSII core proteins D1/D2 and formation of the PSII RC is blocked specifically in the absence of ONE-HELIX PROTEIN1 (OHP1) and OHP2 proteins in Arabidopsis (Arabidopsis thaliana), indicating that OHP1 and OHP2 are essential for the formation of the PSII RC. Mutagenesis of the chlorophyll-binding residues in OHP proteins impairs their function and/or stability, suggesting that they may function in the binding of chlorophyll in vivo. We further show that OHP1, OHP2, and HIGH CHLOROPHYLL FLUORESCENCE244 (HCF244), together with D1, D2, PsbI, and cytochrome b559, form a complex. We designated this complex the PSII RC-like complex to distinguish it from the RC subcomplex in the intact PSII complex. Our data imply that OHP1, OHP2, and HCF244 are present in this PSII RC-like complex for a limited time at an early stage of PSII de novo assembly and of PSII repair under high-light conditions. In a subsequent stage of PSII biogenesis, OHP1, OHP2, and HCF244 are released from the PSII RC-like complex and replaced by the other PSII subunits. Together with previous reports on the cyanobacterium Synechocystis, our results demonstrate that the process of PSII RC assembly is highly conserved among photosynthetic species.
学科主题Plant Sciences
出版地ROCKVILLE
电子版国际标准刊号1532-2548
WOS关键词LIGHT-HARVESTING COMPLEX ; PSBA MESSENGER-RNA ; CHLOROPHYLL BINDING ; AUXILIARY PROTEINS ; CRYSTAL-STRUCTURE ; D1 PROTEIN ; BIOGENESIS ; REPAIR ; STABILITY ; CHLOROPLASTS
WOS研究方向Plant Sciences
语种英语
WOS记录号WOS:000454929100017
出版者AMER SOC PLANT BIOLOGISTS
资助机构National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31470760] ; National Natural Science Foundation for Outstanding YouthNational Natural Science Foundation of China (NSFC) [31322007] ; Shanghai Engineering Research Center of Plant Germplasm Resources [17DZ2252700]
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/19698]  
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, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Shanghai Normal Univ, Coll Life Sci, Shanghai 200234, Peoples R China
5.Langfang Teachers Univ, Coll Life Sci, Langfang 065000, Hebei, Peoples R China
6.Univ Geneva, Dept Plant Biol, CH-1211 Geneva, Switzerland
推荐引用方式
GB/T 7714
Li, Yonghong,Liu, Bei,Zhang, Jiao,et al. OHP1, OHP2, and HCF244 Form a Transient Functional Complex with the Photosystem II Reaction Center[J]. PLANT PHYSIOLOGY,2019,179(1):195-208.
APA Li, Yonghong.,Liu, Bei.,Zhang, Jiao.,Kong, Fanna.,Zhang, Lin.,...&Peng, Lianwei.(2019).OHP1, OHP2, and HCF244 Form a Transient Functional Complex with the Photosystem II Reaction Center.PLANT PHYSIOLOGY,179(1),195-208.
MLA Li, Yonghong,et al."OHP1, OHP2, and HCF244 Form a Transient Functional Complex with the Photosystem II Reaction Center".PLANT PHYSIOLOGY 179.1(2019):195-208.

入库方式: OAI收割

来源:植物研究所

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