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A bestrophin-like protein modulates the proton motive force across the thylakoid membrane in Arabidopsis | |
Duan, Zhikun1; Kong, Fanna1; Zhang, Lin1; Li, Wenjing; Zhang, Jiao; Peng, Lianwei | |
2016 | |
Source Publication | JOURNAL OF INTEGRATIVE PLANT BIOLOGY |
ISSN | 1672-9072 |
Volume | 58Issue:10Pages:848-858 |
Abstract | ur knowl During photosynthesis, photosynthetic electron transport generates a proton motive force (pmf) across the thylakoid membrane, which is used for ATP biosynthesis via ATP synthase in the chloroplast. The pmf is composed of an electric potential () and an osmotic component (pH). Partitioning between these components in chloroplasts is strictly regulated in response to fluctuating environments. However, oedge of the molecular mechanisms that regulate pmf partitioning is limited. Here, we report a bestrophin-like protein (AtBest), which is critical for pmf partitioning. While the pH component was slightly reduced in atbest, the component was much greater in this mutant than in the wild type, resulting in less efficient activation of nonphotochemical quenching (NPQ) upon both illumination and a shift from low light to high light. Although no visible phenotype was observed in the atbest mutant in the greenhouse, this mutant exhibited stronger photoinhibition than the wild type when grown in the field. AtBest belongs to the bestrophin family proteins, which are believed to function as chloride (Cl-) channels. Thus, our findings reveal an important Cl- channel required for ion transport and homeostasis across the thylakoid membrane in higher plants. These processes are essential for fine-tuning photosynthesis under fluctuating environmental conditions. |
Keyword | Bestrophin Cl- channel photoprotection photosynthesis proton motive force |
Subject Area | Biochemistry & Molecular Biology ; Plant Sciences |
DOI | 10.1111/jipb.12475 |
Indexed By | SCI |
Language | 英语 |
WOS Keyword | CHLORIDE CHANNEL ; IN-VIVO ; FAMILY ; PH ; PHOTOPROTECTION ; PHOTOSYNTHESIS ; ELECTRON ; CLONING ; ATCLCE ; ROLES |
WOS Research Area | Science Citation Index Expanded (SCI-EXPANDED) |
WOS ID | WOS:000385427800004 |
Publisher | WILEY |
Subtype | Article |
Publication Place | HOBOKEN |
EISSN | 1744-7909 |
Funding Organization | National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31322007, 31570239] ; Hundred Talents Program of the Chinese Academy of SciencesChinese Academy of Sciences |
Corresponding Author Email | penglianwei@ibcas.ac.cn |
OA | hybrid, Green Published |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | http://ir.ibcas.ac.cn/handle/2S10CLM1/25294 |
Collection | 中科院光生物学重点实验室 |
Affiliation | 1.Chinese Acad Sci, Key Lab Photobiol, CAS Ctr Excellence Mol Plant Sci, Inst Bot, Beijing 100093, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
Recommended Citation GB/T 7714 | Duan, Zhikun,Kong, Fanna,Zhang, Lin,et al. A bestrophin-like protein modulates the proton motive force across the thylakoid membrane in Arabidopsis[J]. JOURNAL OF INTEGRATIVE PLANT BIOLOGY,2016,58(10):848-858. |
APA | Duan, Zhikun,Kong, Fanna,Zhang, Lin,Li, Wenjing,Zhang, Jiao,&Peng, Lianwei.(2016).A bestrophin-like protein modulates the proton motive force across the thylakoid membrane in Arabidopsis.JOURNAL OF INTEGRATIVE PLANT BIOLOGY,58(10),848-858. |
MLA | Duan, Zhikun,et al."A bestrophin-like protein modulates the proton motive force across the thylakoid membrane in Arabidopsis".JOURNAL OF INTEGRATIVE PLANT BIOLOGY 58.10(2016):848-858. |
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Duan-2016-A bestroph(4189KB) | 期刊论文 | 出版稿 | 开放获取 | CC BY-NC-SA | View Application Full Text |
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