Modular arrangements of sequence motifs determine the functional diversity of KDM proteins
文献类型：期刊论文
| 作者 | Wang, Zerong; Liu, Dongyang2; Xu, Baofang; Tian, Ruixia; Zuo, Yongchun |
| 刊名 | BRIEFINGS IN BIOINFORMATICS
 |
| 出版日期 | 2021 |
| 卷号 | 22期号:3 |
| 关键词 | histone methylation KDM proteins arrangements of sequence motifs modular activities evolution |
| ISSN号 | 1467-5463 |
| DOI | 10.1093/bib/bbaa215 |
| 文献子类 | Review |
| 英文摘要 | 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. |
| 学科主题 | Biochemical Research Methods ; Mathematical & Computational Biology |
| 出版地 | OXFORD |
| 电子版国际标准刊号 | 1477-4054 |
| 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) |
| 语种 | 英语 |
| WOS记录号 | WOS:000709461300144 |
| 出版者 | OXFORD UNIV PRESS |
| 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] |
| 源URL | [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.Chinese Acad Sci, Inst Bot, Beijing, Peoples R China 2.Inner Mongolia Univ, Coll Life Sci, State Key Lab Reprod Regulat & Breeding Grassland, Hohhot 010070 9, 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). |
入库方式： OAI收割
来源：植物研究所
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