Modular arrangements of sequence motifs determine the functional diversity of KDM proteins

doi:10.1093/bib/bbaa215

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	Modular arrangements of sequence motifs determine the functional diversity of KDM proteins
	Wang, Zerong ; Liu, Dongyang 1; Xu, Baofang ; Tian, Ruixia ; Zuo, Yongchun
	2021
发表期刊	BRIEFINGS IN BIOINFORMATICS
ISSN	1467-5463
卷号	22 期号:3
摘要	Histone lysine demethylases (KDMs) play a vital role in regulating chromatin dynamics and transcription. KDM proteins are given modular activities by its sequence motifs with obvious roles division, which endow the complex and diverse functions. In our review, according to functional features, we classify sequence motifs into four classes: catalytic motifs, targeting motifs, regulatory motifs and potential motifs. JmjC, as the main catalytic motif, combines to Fe2+ and alpha-ketoglutarate by residues H-D/E-H and S-N-N/Y-K-N/Y-T/S. Targeting motifs make catalytic motifs recognize specific methylated lysines, such as PHD that helps KDM5 to demethylate H3K4me3. Regulatory motifs consist of a functional network. For example, NLS, Ser-rich, TPR and JmjN motifs regulate the nuclear localization. And interactions through the CW-type-C4H2C2-SWIRM are necessary to the demethylase activity of KDM1B. Additionally, many conservative domains that have potential functions but no deep exploration are reviewed for the first time. These conservative domains are usually amino acid-rich regions, which have great research value. The arrangements of four types of sequence motifs generate that KDM proteins diversify toward modular activities and biological functions. Finally, we draw a blueprint of functional mechanisms to discuss the modular activity of KDMs.
关键词	histone methylation KDM proteins arrangements of sequence motifs modular activities evolution
学科领域	Biochemical Research Methods ; Mathematical & Computational Biology
DOI	10.1093/bib/bbaa215
收录类别	SCI
语种	英语
WOS关键词	STRUCTURAL INSIGHTS ; AT-HOOK ; NEURONAL DIFFERENTIATION ; SUBSTRATE-SPECIFICITY ; HISTONE DEMETHYLATION ; NUCLEAR-LOCALIZATION ; CELL-PROLIFERATION ; CHROMATIN-BINDING ; CRYSTAL-STRUCTURE ; GENE-EXPRESSION
WOS研究方向	Science Citation Index Expanded (SCI-EXPANDED)
WOS记录号	WOS:000709461300144
出版者	OXFORD UNIV PRESS
文献子类	Review
出版地	OXFORD
EISSN	1477-4054
资助机构	National Natural Science Foundation of China [61702290, 61861036] ; Program for Young Talents of Science and Technology in Universities of Inner Mongolia Autonomous Region [NJYT-18-B01] ; Fund for Excellent Young Scholars of Inner Mongolia [2017JQ04]
作者邮箱	yczuo@imu.edu.cn
引用统计	被引频次：15[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/2S10CLM1/26569
专题	中科院光生物学重点实验室
作者单位	1.Inner Mongolia Univ, Coll Life Sci, State Key Lab Reprod Regulat & Breeding Grassland, Hohhot 010070 9, Peoples R China 2.Chinese Acad Sci, Inst Bot, Beijing, Peoples R China
推荐引用方式 GB/T 7714	Wang, Zerong,Liu, Dongyang,Xu, Baofang,et al. Modular arrangements of sequence motifs determine the functional diversity of KDM proteins[J]. BRIEFINGS IN BIOINFORMATICS,2021,22(3).
APA	Wang, Zerong,Liu, Dongyang,Xu, Baofang,Tian, Ruixia,&Zuo, Yongchun.(2021).Modular arrangements of sequence motifs determine the functional diversity of KDM proteins.BRIEFINGS IN BIOINFORMATICS,22(3).
MLA	Wang, Zerong,et al."Modular arrangements of sequence motifs determine the functional diversity of KDM proteins".BRIEFINGS IN BIOINFORMATICS 22.3(2021).

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