The N-terminal domain of Lhcb proteins is critical for recognition of the LHCII kinase

doi:10.1016/j.bbabio.2015.10.012

CORC > 植物研究所 > 中国科学院植物研究所 > 中科院光生物学重点实验室

	The N-terminal domain of Lhcb proteins is critical for recognition of the LHCII kinase
	Liu, Wu 1; Tu, Wenfeng ; Liu, Yang 3; Sun, Ruixue ; Liu, Cheng ; Yang, Chunhong
刊名	BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
	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
电子版国际标准刊号	1879-2650
出版地	AMSTERDAM
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
出版者	ELSEVIER SCIENCE BV
WOS记录号	WOS:000366771700009
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]
内容类型	期刊论文
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.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China 2.China Agr Univ, Coll Biol Sci, Key Lab Agrobiotechnol, Beijing 100193, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, 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.