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The impact of N-terminal phosphorylation on LHCII conformation in state transition
Ding JH(丁锦鸿); Li N(李宁); Wang ML; Zhang Y(章燕); Lv SQ(吕守芹); Long M(龙勉); Lu, SQ (reprint author), Chinese Acad Sci, Natl Micrograv Lab, Key Lab Micrograv, Beijing 100190, Peoples R China.
Source PublicationActa Mechanica Sinica
2014-06
Volume30Issue:3Pages:447-456
ISSN0567-7718
AbstractState transition is an important protection mechanism of plants for maintaining optimal efficiency through redistributing unbalanced excitation energy between photo-system II (PSII) and photosystem I (PSI). This process depends on the reversible phosphorylation/dephosphorylation of the major light-harvesting complex II (LHCII) and its bi-directional migration between PSII and PSI. But it remains unclear how phosphorylation/dephosphorylation modulates the LHCII conformation and further regulates its reversible migration. Here molecular dynamics simulations (MDS) were employed to elucidate the impact of phosphorylation on LHCII conformation. The results indicated that N-terminal phosphorylation loosened LHCII trimer with decreased hydrogen bond (H-bond) interactions and extended the distances between neighboring monomers, which stemmed from the conformational adjustment of each monomer itself. Global conformational change of LHCII monomer started from its stromal Nterminal (including the phosphorylation sites) by enhancing its interaction to lipid membrane and by adjusting the interaction network with surrounded inter-monomer and intra-monomer transmembrane helixes of B, C, and A, and finally triggered the reorientation of transmembrane helixes and transferred the conformational change to luminal side helixes and loops. These results further our understanding in molecular mechanism of LHCII migration during state transition from the phosphorylation-induced microstructural feature of LHCII.
KeywordState Transition Lhcii Phosphorylation Conformation
Subject AreaEngineering ; Mechanics
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Indexed BySCI ; EI ; CSCD
Language英语
WOS IDWOS:000338236800019
Funding OrganizationThe project was supported by the National Key Basic Research Foundation of China (2006CB910303 and 2011CB710904), the National Natural Science Foundation of China (11072251 and 31230027), the CAS Knowledge Innovation Program (KJCX2-YW-L08), and the Scientific Research Equipment Project (Y2010030).
DepartmentNML分子-细胞生物力学与空间生命科学
Classification二类
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Cited Times:4[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://dspace.imech.ac.cn/handle/311007/49033
Collection国家微重力实验室
Corresponding AuthorLu, SQ (reprint author), Chinese Acad Sci, Natl Micrograv Lab, Key Lab Micrograv, Beijing 100190, Peoples R China.
Recommended Citation
GB/T 7714
Ding JH,Li N,Wang ML,et al. The impact of N-terminal phosphorylation on LHCII conformation in state transition[J]. Acta Mechanica Sinica,2014,30(3):447-456.
APA Ding JH.,Li N.,Wang ML.,Zhang Y.,Lv SQ.,...&Lu, SQ .(2014).The impact of N-terminal phosphorylation on LHCII conformation in state transition.Acta Mechanica Sinica,30(3),447-456.
MLA Ding JH,et al."The impact of N-terminal phosphorylation on LHCII conformation in state transition".Acta Mechanica Sinica 30.3(2014):447-456.
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