The impact of N-terminal phosphorylation on LHCII conformation in state transition | |
Ding JH(丁锦鸿)![]() ![]() ![]() ![]() | |
Source Publication | Acta Mechanica Sinica
![]() |
2014-06 | |
Volume | 30Issue:3Pages:447-456 |
ISSN | 0567-7718 |
Abstract | State 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. |
Keyword | State Transition Lhcii Phosphorylation Conformation |
Subject Area | Engineering ; Mechanics |
URL | 查看原文 |
Indexed By | SCI ; EI ; CSCD |
Language | 英语 |
WOS ID | WOS:000338236800019 |
Funding Organization | The 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). |
Department | NML分子-细胞生物力学与空间生命科学 |
Classification | 二类 |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | http://dspace.imech.ac.cn/handle/311007/49032 |
Collection | 微重力重点实验室 |
Corresponding Author | Lu, 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. |
Files in This Item: | Download All | |||||
File Name/Size | DocType | Version | Access | License | ||
IMCAS-J2014-176.pdf(746KB) | 期刊论文 | 作者接受稿 | 开放获取 | CC BY-NC-SA | View Download |
Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Edit Comment