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Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans
Yang, Y; Hu, LL; Wang, P; Hou, HF; Lin, Y; Liu, Y; Li, Z; Gong, R; Feng, XA; Zhou, L; Zhang, W; Dong, YH; Yang, HR; Lin, HQ; Wang, YQ; Chen, CD; Xu, YH; Dong YH(董宇辉)
2010
发表期刊CELL RESEARCH
卷号20期号:8页码:886-898
通讯作者[Lin, Hanqing ; Wang, Yiqin ; Chen, Charlie Degui] Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Shanghai Key Lab Mol Androl,State Key Lab Mol Bio, Shanghai 200031, Peoples R China ; [Zhou, Lu] Fudan Univ, Sch Pharm, Shanghai 201203, Peoples R China ; [Hou, Haifeng ; Dong, Yuhui] Chinese Acad Sci, Inst High Energy Phys, Beijing Synchrotron Radiat Facil, Beijing 100049, Peoples R China ; [Yang, Ying ; Hu, Lulu ; Wang, Ping ; Lin, Yan ; Liu, Yi ; Li, Ze ; Gong, Rui ; Zhang, Wen ; Yang, Huirong ; Xu, Yanhui] Fudan Univ, Inst Biomed Sci, Shanghai 200032, Peoples R China ; [Yang, Ying ; Hu, Lulu ; Wang, Ping ; Lin, Yan ; Liu, Yi ; Li, Ze ; Gong, Rui ; Feng, Xiang ; Zhang, Wen ; Yang, Huirong ; Xu, Yanhui] Fudan Univ, Sch Life Sci, Shanghai 200433, Peoples R China ; [Yang, Ying ; Xu, Yanhui] Fudan Univ, Shanghai Med Coll, Dept Oncol, Shanghai 200032, Peoples R China ; [Yang, Ying ; Xu, Yanhui] Fudan Univ, Inst Canc, Shanghai Canc Ctr, Shanghai 200032, Peoples R China
文章类型Article
摘要Histone lysine methylation can be removed by JmjC domain-containing proteins in a sequence-and methylation-state-specific manner. However, how substrate specificity is determined and how the enzymes are regulated were largely unknown. We recently found that ceKDM7A, a PHD- and JmjC domain-containing protein, is a histone demethylase specific for H3K9me2 and H3K27me2, and the PHD finger binding to H3K4me3 guides the demethylation activity in vivo. To provide structural insight into the molecular mechanisms for the enzymatic activity and the function of the PHD finger, we solved six crystal structures of the enzyme in apo form and in complex with single or two peptides containing various combinations of H3K4me3, H3K9me2, and H3K27me2 modifications. The structures indicate that H3K9me2 and H3K27me2 interact with ceKDM7A in a similar fashion, and that the peptide-binding specificity is determined by a network of specific interactions. The geometrical measurement of the structures also revealed that H3K4me3 associated with the PHD finger and H3K9me2 bound to the JmjC domain are from two separate molecules, suggesting a trans-histone peptide-binding mechanism. Thus, our systemic structural studies reveal not only the substrate recognition by the catalytic domain but also more importantly, the molecular mechanism of dual specificity of ceDKM7A for both H3K9me2 and H3K27me2.
关键词histone methylation demethylase structure PHD JmjC
学科领域Cell Biology
研究领域[WOS]Cell Biology ; Cell Biology
DOI10.1038/cr.2010.86
URL查看原文
语种英语
研究领域[WOS]Cell Biology ; Cell Biology
WOS类目Cell Biology
WOS记录号WOS:000280563100006
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被引频次:36[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/238681
专题多学科研究中心
作者单位中国科学院高能物理研究所
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GB/T 7714
Yang, Y,Hu, LL,Wang, P,et al. Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans[J]. CELL RESEARCH,2010,20(8):886-898.
APA Yang, Y.,Hu, LL.,Wang, P.,Hou, HF.,Lin, Y.,...&董宇辉.(2010).Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans.CELL RESEARCH,20(8),886-898.
MLA Yang, Y,et al."Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans".CELL RESEARCH 20.8(2010):886-898.
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