The impact of N-terminal phosphorylation on LHCII conformation in state transition
文献类型：期刊论文
| 作者 | 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.
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| 刊名 | Acta Mechanica Sinica
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| 出版日期 | 2014-06 |
| 卷号 | 30期号:3页码:447-456 |
| 关键词 | State Transition Lhcii Phosphorylation Conformation |
| ISSN号 | 0567-7718 |
| 产权排序 | [Ding, Jin-Hong; Li, Ning; Wang, Man-Liu; Zhang, Yan; Lu, Shou-Qin; Long, Mian] Chinese Acad Sci, Natl Micrograv Lab, Key Lab Micrograv, Beijing 100190, Peoples R China; [Ding, Jin-Hong; Li, Ning; Wang, Man-Liu; Zhang, Yan; Lu, Shou-Qin; Long, Mian] Chinese Acad Sci, Inst Mech, Ctr Biomech & Bioengn, Beijing 100190, Peoples R China |
| 文献子类 | Article |
| 英文摘要 | 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. |
| 学科主题 | Engineering ; Mechanics |
| 分类号 | 二类 |
| URL标识 | 查看原文 |
| 语种 | 英语 |
| WOS记录号 | WOS:000338236800019 |
| 资助机构 | 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). |
| 公开日期 | 2014-09-03 |
| 源URL | [http://dspace.imech.ac.cn/handle/311007/49033]  |
| 专题 | 力学研究所_国家微重力实验室 |
| 通讯作者 | Lu, SQ (reprint author), Chinese Acad Sci, Natl Micrograv Lab, Key Lab Micrograv, Beijing 100190, Peoples R China. |
| 推荐引用方式 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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来源：力学研究所
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