The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex

doi:10.1093/nar/gkz819

	The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex
	Han, Jianming 1,2; Li, Tingting 1,2; Li, Yanjing 1,2; Li, Muchun3 ; Wang, Xiaoman 1,2; Peng, Chao 4; Su, Chen 4; Li, Na 4; Li, Yiwen 4; Xu, Ying 1,2; Chen, Yong1,2,3,5
	2019-11-04
发表期刊	NUCLEIC ACIDS RESEARCH
ISSN	0305-1048
EISSN	1362-4962
卷号	47 期号:19 页码:10426-10438
发表状态	已发表
DOI	10.1093/nar/gkz819
摘要	The Mixed Lineage Leukemia protein 1 (MLL1) plays an essential role in the maintenance of the histone H3 lysine 4 (H3K4) methylation status for gene expression during differentiation and development. The methyltransferase activity of MLL1 is regulated by three conserved core subunits, WDR5, RBBP5 and ASH2L. Here, we determined the structure of human RBBP5 and demonstrated its role in the assembly and regulation of the MLL1 complex. We identified an internal interaction between the WD40 propeller and the C-terminal distal region in RBBP5, which assisted the maintenance of the compact conformation of the MLL1 complex. We also discovered a vertebrate-specific motif in the C-terminal distal region of RBBP5 that contributed to nucleosome recognition and methylation of nucleosomes by the MLL1 complex. Our results provide new insights into functional conservation and evolutionary plasticity of the scaffold protein RBBP5 in the regulation of KMT2-family methyltransferase complexes.
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收录类别	SCI ; SCIE
语种	英语
资助项目	Strategic Priority Research Program of the Chinese Academy of Sciences[XDB08010201]
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
WOS记录号	WOS:000496767900041
出版者	OXFORD UNIV PRESS
WOS关键词	HISTONE H3K4 METHYLASES ; COMPASS FAMILY ; DATA REDUCTION ; SCATTERING ; DOMAIN ; MODEL
原始文献类型	Article
引用统计
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/102249
专题	生命科学与技术学院_硕士生生命科学与技术学院_特聘教授组_陈勇组
通讯作者	Chen, Yong
作者单位	1.Chinese Acad Sci, State Key Lab Mol Biol, Natl Ctr Prot Sci Shanghai, CAS Ctr Excellence Mol Cell Sci,Shanghai Inst Bio, 333 Haike Rd, Shanghai 201210, Peoples R China 2.Univ Chinese Acad Sci, 333 Haike Rd, Shanghai 201210, Peoples R China 3.Shanghai Tech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai 201210, Peoples R China 4.Zhangjiang Lab, Natl Facil Prot Sci Shanghai, Shanghai 201210, Peoples R China 5.Chinese Acad Sci, Shanghai Sci Res Ctr, Shanghai 201204, Peoples R China
通讯作者单位	生命科学与技术学院
推荐引用方式 GB/T 7714	Han, Jianming,Li, Tingting,Li, Yanjing,et al. The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex[J]. NUCLEIC ACIDS RESEARCH,2019,47(19):10426-10438.
APA	Han, Jianming.,Li, Tingting.,Li, Yanjing.,Li, Muchun.,Wang, Xiaoman.,...&Chen, Yong.(2019).The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex.NUCLEIC ACIDS RESEARCH,47(19),10426-10438.
MLA	Han, Jianming,et al."The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex".NUCLEIC ACIDS RESEARCH 47.19(2019):10426-10438.