中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition

文献类型:期刊论文

作者Fang, Jian1,2,3; Cheng, Jingdong1; Wang, Jiaolong4; Zhang, Qiao5,6; Liu, Mengjie1; Gong, Rui1; Wang, Ping1; Zhang, Xiaodan1; Feng, Yangyang1; Lan, Wenxian4
刊名NATURE COMMUNICATIONS
出版日期2016-04-01
卷号7
英文摘要UHRF1 is an important epigenetic regulator for maintenance DNA methylation. UHRF1 recognizes hemi-methylated DNA (hm-DNA) and trimethylation of histone H3K9 (H3K9me3), but the regulatory mechanism remains unknown. Here we show that UHRF1 adopts a closed conformation, in which a C-terminal region (Spacer) binds to the tandem Tudor domain (TTD) and inhibits H3K9me3 recognition, whereas the SET-and-RING-associated (SRA) domain binds to the plant homeodomain (PHD) and inhibits H3R2 recognition. Hm-DNA impairs the intramolecular interactions and promotes H3K9me3 recognition by TTD-PHD. The Spacer also facilitates UHRF1-DNMT1 interaction and enhances hm-DNA-binding affinity of the SRA. When TTD-PHD binds to H3K9me3, SRA-Spacer may exist in a dynamic equilibrium: either recognizes hm-DNA or recruits DNMT1 to chromatin. Our study reveals the mechanism for regulation of H3K9me3 and hm-DNA recognition by URHF1.
WOS标题词Science & Technology
类目[WOS]Multidisciplinary Sciences
研究领域[WOS]Science & Technology - Other Topics
关键词[WOS]EPIGENETIC REGULATOR UHRF1 ; SRA DOMAIN ; MAMMALIAN DEVELOPMENT ; BINDING-PROTEIN ; GENE-EXPRESSION ; METHYLTRANSFERASE DNMT1 ; STRUCTURAL BASIS ; TANDEM TUDOR ; PHD FINGER ; H3 TAIL
收录类别SCI
语种英语
WOS记录号WOS:000373621000001
源URL[http://ir.wipm.ac.cn/handle/112942/9316]  
专题武汉物理与数学研究所_磁共振应用研究部
作者单位1.Fudan Univ, Shanghai Med Coll, Sch Basic Med Sci, Key Lab Mol Med,Minist Educ,Dept Syst Biol Med, Shanghai 200032, Peoples R China
2.Fudan Univ, Sch Life Sci, Collaborat Innovat Ctr Genet & Dev, State Key Lab Genet Engn, Shanghai 200433, Peoples R China
3.Fudan Univ, Shanghai Med Coll, Shanghai Canc Ctr, Inst Biomed Sci, Shanghai 200032, Peoples R China
4.Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, 345 LingLing Rd, Shanghai 200032, Peoples R China
5.E China Normal Univ, Inst Biomed Sci, Shanghai Key Lab Regulatory Biol, Shanghai 200241, Peoples R China
6.E China Normal Univ, Sch Life Sci, Shanghai 200241, Peoples R China
7.Chinese Acad Sci, Wuhan Inst Phys & Math, State Key Lab Magnet Resonance & Atom & Mol Phys, Wuhan 430071, Peoples R China
推荐引用方式
GB/T 7714
Fang, Jian,Cheng, Jingdong,Wang, Jiaolong,et al. Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition[J]. NATURE COMMUNICATIONS,2016,7.
APA Fang, Jian.,Cheng, Jingdong.,Wang, Jiaolong.,Zhang, Qiao.,Liu, Mengjie.,...&Xu, Yanhui.(2016).Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition.NATURE COMMUNICATIONS,7.
MLA Fang, Jian,et al."Hemi-methylated DNA opens a closed conformation of UHRF1 to facilitate its histone recognition".NATURE COMMUNICATIONS 7(2016).

入库方式: OAI收割

来源:武汉物理与数学研究所

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