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题名: Cooperative Action between SALL4A and TET Proteins in Stepwise Oxidation of 5-Methylcytosine
作者: Xiong, Jun; Zhang, Zhuqiang; Chen, Jiayu; Huang, Hua; Xu, Yali; Ding, Xiaojun; Zheng, Yong; Nishinakamura, Ryuichi; Xu, Guo-Liang; Wang, Hailin; Chen, She; Gao, Shaorong; Zhu, Bing
刊名: MOLECULAR CELL
出版日期: 2016-12-01
卷号: 64, 期号:5, 页码:913-925
DOI: 10.1016/j.molcel.2016.10.013
部门归属: 环境化学与生态毒理学国家重点实验室
英文摘要: TET family enzymes successively oxidize 5-methylcytosine to 5-hydroxymethylcytosine, 5-formylcytosine, and 5-carboxylcytosine, leading to eventual demethylation. 5hmC and TET enzymes occupy distinct chromatin regions, suggesting unknown mechanisms controlling the fate of 5hmC within diverse chromatin environments. Here, we report that SALL4A preferentially associates with 5hmC in vitro and occupies enhancers in mouse embryonic stem cells in a largely TET1-dependent manner. Although most 5hmC at SALL4A peaks undergoes further oxidation, this process is abrogated upon deletion of Sall4 gene, with a concomitant reduction of TET2 at these regions. Thus, SALL4A facilitates further oxidation of 5hmC at its binding sites, which requires its 5hmC-binding activity and TET2, supporting a collaborative action between SALL4A and TET proteins in regulating stepwise oxidation of 5mC at enhancers. Our study identifies SALL4A as a 5hmC binder, which facilitates 5hmC oxidation by stabilizing TET2 association, thereby fine-tuning expression profiles of developmental genes in mouse embryonic stem cells.
收录类别: SCI
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内容类型: 期刊论文
URI标识: http://ir.rcees.ac.cn/handle/311016/35824
Appears in Collections:环境化学与生态毒理学国家重点实验室_期刊论文

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