The N-terminal domain of Lhcb proteins is critical for recognition of the LHCII kinase
文献类型：期刊论文
| 作者 | Liu, Wu2; Tu, Wenfeng; Liu, Yang1; Sun, Ruixue; Liu, Cheng; Yang, Chunhong |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
 |
| 出版日期 | 2016 |
| 卷号 | 1857期号:1页码:79-88 |
| 关键词 | Light harvesting complex Kinase N-terminal Protein interactions |
| ISSN号 | 0005-2728 |
| DOI | 10.1016/j.bbabio.2015.10.012 |
| 文献子类 | Article |
| 英文摘要 | The light-harvesting chlorophyll (Chi) a/b complex of photosystem (PS) II (LHCII) plays important roles in the distribution of the excitation energy between the two PSs in the thylakoid membrane during state transitions. In this process, LHCII, homo- or heterotrimers composed of Lhcb1-3, migrate between PSII and PSI depending on the phosphorylation status of Lhcb1 and Lhcb2. We have studied the mechanisms of the substrate recognition of a thylakoid threonine kinase using reconstituted site-directed trimeric Lhcb protein-pigment complex mutants. Mutants lacking the positively charged residues R/K upstream of phosphorylation site (Thr) in the N-terminal domain of Lhcb1 were no longer phosphorylated. Besides, the length of the peptide upstream of the phosphorylated site (Thr) is also crucial for Lhcb phosphorylation in vitro. Furthermore, the two N-terminal residues of Lhcb appear to play a key role in the phosphorylation kinetics because Lhcb with N-terminal RR was phosphorylated much faster than with RK Therefore, we conclude that the substrate recognition of the LHCII kinase is determined to a large extent by the N-terminal sequence of the Lhcb proteins. The study provides new insights into the interactions of the Lhcb proteins with the LHCII kinase. (C) 2015 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology ; Biophysics |
| 出版地 | AMSTERDAM |
| 电子版国际标准刊号 | 1879-2650 |
| WOS关键词 | LIGHT-HARVESTING-COMPLEX ; PHOTOSYSTEM-II ; STATE TRANSITIONS ; SUBSTRATE-SPECIFICITY ; SIGNALING SPECIFICITY ; CATALYTIC SUBUNIT ; CRYSTAL-STRUCTURE ; STRUCTURAL BASIS ; PHOSPHORYLATION ; SITE |
| WOS研究方向 | Science Citation Index Expanded (SCI-EXPANDED) |
| 语种 | 英语 |
| WOS记录号 | WOS:000366771700009 |
| 出版者 | ELSEVIER SCIENCE BV |
| 资助机构 | National Basic Research Program of ChinaNational Basic Research Program of China [2011CBA00904] ; Key Research Program of the Chinese Academy of Sciences Grant [KSZD-EW-Z-018, KGZD-EW-T05] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31370275, 31570236] |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/25330]  |
| 专题 | 中科院光生物学重点实验室 |
| 作者单位 | 1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 2.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China 3.China Agr Univ, Coll Biol Sci, Key Lab Agrobiotechnol, Beijing 100193, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Wu,Tu, Wenfeng,Liu, Yang,et al. The N-terminal domain of Lhcb proteins is critical for recognition of the LHCII kinase[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,2016,1857(1):79-88. |
| APA | Liu, Wu,Tu, Wenfeng,Liu, Yang,Sun, Ruixue,Liu, Cheng,&Yang, Chunhong.(2016).The N-terminal domain of Lhcb proteins is critical for recognition of the LHCII kinase.BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS,1857(1),79-88. |
| MLA | Liu, Wu,et al."The N-terminal domain of Lhcb proteins is critical for recognition of the LHCII kinase".BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1857.1(2016):79-88. |
入库方式： OAI收割
来源：植物研究所
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