Nickel(II) Inhibits Tet-Mediated 5-Methylcytosine Oxidation by High Affinity Displacement of the Cofactor Iron(II)
文献类型：期刊论文
| 作者 | Yin, Ruichuan; Mo, Jiezhen; Dai, Jiayin; Wang, Hailin |
| 刊名 | ACS CHEMICAL BIOLOGY
 |
| 出版日期 | 2017-12-01 |
| 卷号 | 12期号:6页码:1494-1498 |
| 英文摘要 | Ten-eleven translocation (Tet) family proteins are Fe(II)- and 2-oxoglutarate-dependent dioxygenases that regulate the dynamics of DNA methylation by catalyzing the oxidation of DNA 5-methylcytosine (5mC). To exert physiologically important functions, redox-active iron chelated in the catalytic center of Tet proteins directly involves the oxidation of the multiple substrates. To understand the function and interaction network of Tet dioxygenases, it is interesting to obtain high affinity and a specific inhibitor. Surprisingly, here we found that natural Ni(II) ion can bind to the Fe(II)-chelating motif (HXD) with an affinity of 7.5-fold as high as Fe(II). Consistently, we further found that Ni(II) ion can displace the cofactor Fe(II) of Tet dioxygenases and inhibit Tet-mediated 5mC oxidation activity with an estimated IC50 of 1.2 mu M. Essentially, Ni(II) can be used as a high affinity and selective inhibitor to explore the function and dynamics of Tet proteins. |
| 源URL | [http://ir.rcees.ac.cn/handle/311016/39369]  |
| 专题 | 生态环境研究中心_环境化学与生态毒理学国家重点实验室 |
| 推荐引用方式 GB/T 7714 | Yin, Ruichuan,Mo, Jiezhen,Dai, Jiayin,et al. Nickel(II) Inhibits Tet-Mediated 5-Methylcytosine Oxidation by High Affinity Displacement of the Cofactor Iron(II)[J]. ACS CHEMICAL BIOLOGY,2017,12(6):1494-1498. |
| APA | Yin, Ruichuan,Mo, Jiezhen,Dai, Jiayin,&Wang, Hailin.(2017).Nickel(II) Inhibits Tet-Mediated 5-Methylcytosine Oxidation by High Affinity Displacement of the Cofactor Iron(II).ACS CHEMICAL BIOLOGY,12(6),1494-1498. |
| MLA | Yin, Ruichuan,et al."Nickel(II) Inhibits Tet-Mediated 5-Methylcytosine Oxidation by High Affinity Displacement of the Cofactor Iron(II)".ACS CHEMICAL BIOLOGY 12.6(2017):1494-1498. |
入库方式： OAI收割
来源：生态环境研究中心
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。