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The N-terminal domain of Lhcb proteins is critical for recognition of the LHCII kinase
Liu, Wu1; Tu, Wenfeng; Liu, Yang2; Sun, Ruixue; Liu, Cheng; Yang, Chunhong
2016
发表期刊BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
ISSN0005-2728
卷号1857期号:1页码:79-88
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.
关键词Light harvesting complex Kinase N-terminal Protein interactions
学科领域Biochemistry & Molecular Biology ; Biophysics
DOI10.1016/j.bbabio.2015.10.012
收录类别SCI
语种英语
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)
WOS记录号WOS:000366771700009
出版者ELSEVIER SCIENCE BV
文献子类Article
出版地AMSTERDAM
EISSN1879-2650
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]
作者邮箱yangch@ibcas.ac.cn
作品OA属性Bronze
引用统计
被引频次:5[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符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.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.China Agr Univ, Coll Biol Sci, Key Lab Agrobiotechnol, Beijing 100193, Peoples R China
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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.
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