IB-CAS  > 中科院光生物学重点实验室
Structural basis for energy and electron transfer of the photosystem I-IsiA-flavodoxin supercomplex
Cao, Peng; Cao, Duanfang; Si, Long1; Su, Xiaodong; Tian, Lijin2; Chang, Wenrui1; Liu, Zhenfeng1; Zhang, Xinzheng1,3; Li, Mei
2020
Source PublicationNATURE PLANTS
ISSN2055-026X
Volume6Issue:2Pages:167-176
AbstractCyanobacterial photosystem I supercomplexes bind to iron-stress-induced proteins IsiA and flavodoxin under iron-deficiency conditions. They form a network that is highly efficient at light harvesting and retains normal electron transport efficiency. Under iron-deficiency stress, which occurs frequently in natural aquatic environments, cyanobacteria reduce the amount of iron-enriched proteins, including photosystem I (PSI) and ferredoxin (Fd), and upregulate the expression of iron-stress-induced proteins A and B (IsiA and flavodoxin (Fld)). Multiple IsiAs function as the peripheral antennae that encircle the PSI core, whereas Fld replaces Fd as the electron receptor of PSI. Here, we report the structures of the PSI3-IsiA(18)-Fld(3) and PSI3-IsiA(18) supercomplexes from Synechococcus sp. PCC 7942, revealing features that are different from the previously reported PSI structures, and a sophisticated pigment network that involves previously unobserved pigment molecules. Spectroscopic results demonstrated that IsiAs are efficient light harvesters for PSI. Three Flds bind symmetrically to the trimeric PSI core-we reveal the detailed interaction and the electron transport path between PSI and Fld. Our results provide a structural basis for understanding the mechanisms of light harvesting, energy transfer and electron transport of cyanobacterial PSI under stressed conditions.
Subject AreaPlant Sciences
DOI10.1038/s41477-020-0593-7
Indexed BySCI
Language英语
WOS KeywordCHLOROPHYLL-BINDING-PROTEIN ; ABSORPTION CROSS-SECTION ; IRON-DEFICIENCY ; ANTENNA RING ; WILD-TYPE ; STRESS ; COMPLEX ; PSI ; SUBUNIT ; CP43'
WOS Research AreaPlant Sciences
WOS IDWOS:000512529000005
PublisherNATURE RESEARCH
SubtypeArticle
Publication PlaceBERLIN
EISSN2055-0278
Funding OrganizationNational Key R&D Program of China [2017YFA0503702, 2017YFA0504700] ; Strategic Priority Research Program of CAS [XDB27020106, XDB08020302, XDB08030204] ; Key Research Program of Frontier Sciences of CAS [QYZDB-SSW-SMC005] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31930064, 31770778, 31570724, 31700649] ; National Thousand (Young) Talents Program from the Office of Global Experts Recruitment in China
Corresponding Author Emailxzzhang@ibp.ac.cn ; meili@ibp.ac.cn
Citation statistics
Cited Times:17[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ibcas.ac.cn/handle/2S10CLM1/21919
Collection中科院光生物学重点实验室
Affiliation1.Chinese Acad Sci, CAS Ctr Excellence Biomacromol, Inst Biophys, Natl Lab Biomacromol, Beijing, Peoples R China
2.Univ Chinese Acad Sci, Beijing, Peoples R China
3.Chinese Acad Sci, Inst Bot, Beijing, Peoples R China
4.Chinese Acad Sci, Ctr Biol Imaging, CAS Ctr Excellence Biomacromol, Inst Biophys, Beijing, Peoples R China
Recommended Citation
GB/T 7714
Cao, Peng,Cao, Duanfang,Si, Long,et al. Structural basis for energy and electron transfer of the photosystem I-IsiA-flavodoxin supercomplex[J]. NATURE PLANTS,2020,6(2):167-176.
APA Cao, Peng.,Cao, Duanfang.,Si, Long.,Su, Xiaodong.,Tian, Lijin.,...&Li, Mei.(2020).Structural basis for energy and electron transfer of the photosystem I-IsiA-flavodoxin supercomplex.NATURE PLANTS,6(2),167-176.
MLA Cao, Peng,et al."Structural basis for energy and electron transfer of the photosystem I-IsiA-flavodoxin supercomplex".NATURE PLANTS 6.2(2020):167-176.
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