南方科技大学知识苑(SUSTech KC): Structural basis for the recognition of methylated histone H3 by the Arabidopsis LHP1 chromodomain

题名	Structural basis for the recognition of methylated histone H3 by the Arabidopsis LHP1 chromodomain
作者	Liu，Yanli 1; Yang，Xiajie 2; Zhou，Mengqi 2; Yang，Yinxue 1; Li，Fangzhou 2; Yan，Xuemei 1; Zhang，Mengmeng 1; Wei，Zhengguo 3; Qin，Su4 ; Min，Jinrong 2
通讯作者	Liu，Yanli; Min，Jinrong
发表日期	2022-03-01
DOI	10.1016/j.jbc.2022.101623
发表期刊	JOURNAL OF BIOLOGICAL CHEMISTRY 影响因子和分区
EISSN	1083-351X
卷号	298 期号:3
摘要	Arabidopsis LHP1 (LIKE HETEROCHROMATIN PROTEIN 1), a unique homolog of HP1 in Drosophila, plays important roles in plant development, growth, and architecture. In contrast to specific binding of the HP1 chromodomain to methylated H3K9 histone tails, the chromodomain of LHP1 has been shown to bind to both methylated H3K9 and H3K27 histone tails, and LHP1 carries out its function mainly via its interaction with these two epigenetic marks. However, the molecular mechanism for the recognition of methylated histone H3K9/27 by the LHP1 chromodomain is still unknown. In this study, we characterized the binding ability of LHP1 to histone H3K9 and H3K27 peptides and found that the chromodomain of LHP1 binds to histone H3K9me2/3 and H3K27me2/3 peptides with comparable affinities, although it exhibited no binding or weak binding to unmodified or monomethylated H3K9/K27 peptides. Our crystal structures of the LHP1 chromodomain in peptide-free and peptide-bound forms coupled with mutagenesis studies reveal that the chromodomain of LHP1 bears a slightly different chromodomain architecture and recognizes methylated H3K9 and H3K27 peptides via a hydrophobic clasp, similar to the chromodomains of human Polycomb proteins, which could not be explained only based on primary structure analysis. Our binding and structural studies of the LHP1 chromodomain illuminate a conserved ligand interaction mode between chromodomains of both animals and plants, and shed light on further functional study of the LHP1 protein.
相关链接	[来源记录]
收录类别	SCI ; EI
语种	英语
重要成果	NI论文
学校署名	其他
资助项目	National Natural Science Foundation of China[31500615] ; Sixtalent Professorship of Jiangsu province, China[SWYY-104]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000821051800006
出版者	ELSEVIER
EI入藏号	20220811702630
EI主题词	Crystal structure ; Plants (botany)
EI分类号	Biology:461.9 ; Crystal Lattice:933.1.1
ESI学科分类	BIOLOGY & BIOCHEMISTRY
Scopus记录号	2-s2.0-85125008479
来源库	Web of Science
引用统计	被引频次[WOS]：6
成果类型	期刊论文
条目标识符	http://sustech.caswiz.com/handle/2SGJ60CL/327712
专题	南方科技大学
作者单位	1.College of Pharmaceutical Sciences,Soochow University,Suzhou,Jiangsu,China 2.Hubei Key Laboratory of Genetic Regulation and Integrative Biology,School of Life Sciences,Central China Normal University,Wuhan,Hubei,China 3.School of Biology and Basic Medical Science,Soochow University,Suzhou,Jiangsu,China 4.Life Science Research Center,Southern University of Science and Technology,Shenzhen,Guangdong,China
推荐引用方式 GB/T 7714	Liu，Yanli,Yang，Xiajie,Zhou，Mengqi,et al. Structural basis for the recognition of methylated histone H3 by the Arabidopsis LHP1 chromodomain[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2022,298(3).
APA	Liu，Yanli.,Yang，Xiajie.,Zhou，Mengqi.,Yang，Yinxue.,Li，Fangzhou.,...&Min，Jinrong.(2022).Structural basis for the recognition of methylated histone H3 by the Arabidopsis LHP1 chromodomain.JOURNAL OF BIOLOGICAL CHEMISTRY,298(3).
MLA	Liu，Yanli,et al."Structural basis for the recognition of methylated histone H3 by the Arabidopsis LHP1 chromodomain".JOURNAL OF BIOLOGICAL CHEMISTRY 298.3(2022).