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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 PublicationJOURNAL OF INTEGRATIVE PLANT BIOLOGY
ISSN1672-9072
Volume58Issue:10Pages:848-858
Abstractur 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.
KeywordBestrophin Cl- channel photoprotection photosynthesis proton motive force
Subject AreaBiochemistry & Molecular Biology ; Plant Sciences
DOI10.1111/jipb.12475
Indexed BySCI
Language英语
WOS KeywordCHLORIDE CHANNEL ; IN-VIVO ; FAMILY ; PH ; PHOTOPROTECTION ; PHOTOSYNTHESIS ; ELECTRON ; CLONING ; ATCLCE ; ROLES
WOS Research AreaScience Citation Index Expanded (SCI-EXPANDED)
WOS IDWOS:000385427800004
PublisherWILEY
SubtypeArticle
Publication PlaceHOBOKEN
EISSN1744-7909
Funding OrganizationNational 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 Emailpenglianwei@ibcas.ac.cn
OAhybrid, Green Published
Citation statistics
Cited Times:55[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ibcas.ac.cn/handle/2S10CLM1/25294
Collection中科院光生物学重点实验室
Affiliation1.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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