Structural Insight into Recognition of Methylated Histone Tails by Retinoblastoma-binding Protein 1
文献类型：期刊论文
| 作者 | Gong, Weibin1; Zhou, Tao1; Mo, Jinjin1,2; Perrett, Sarah1; Wang, Jinfeng1; Feng, Yingang1,3
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| 刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
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| 出版日期 | 2012-03-09 |
| 卷号 | 287期号:11页码:8531-8540 |
| 英文摘要 | Retinoblastoma-binding protein 1 (RBBP1), also named AT-rich interaction domain containing 4A (ARID4A), is a tumor and leukemia suppressor involved in epigenetic regulation in leukemia and Prader-Willi/Angelman syndromes. Although the involvement in epigenetic regulation is proposed to involve its chromobarrel and/or Tudor domains because of their potential binding to methylated histone tails, the structures of these domains and their interactions with methylated histone tails are still uncharacterized. In this work, we first found that RBBP1 contains five domains by bioinformatics analysis. Three of the five domains, i.e. chromobarrel, Tudor, and PWWP domains, are Royal Family domains, which potentially bind to methylated histone tails. We further purified these domains and characterized their interaction with methylated histone tails by NMR titration experiments. Among the three Royal Family domains, only the chromobarrel domain could recognize trimethylated H4K20 (with an affinity of similar to 3 mM), as well as recognizing trimethylated H3K9, H3K27, and H3K36 (with lower affinities). The affinity could be further enhanced up to 15-fold by the presence of DNA. The structure of the chromobarrel domain of RBBP1 determined by NMR spectroscopy has an aromatic cage. Mutagenesis analysis identified four aromatic residues of the cage as the key residues for methylated lysine recognition. Our studies indicate that the chromobarrel domain of RBBP1 is responsible for recognizing methylated histone tails in chromatin remodeling and epigenetic regulation, which presents a significant advance in our understanding of the mechanism and relationship between RBBP1-related gene suppression and epigenetic regulation. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | DEACETYLASE COMPLEX ; MACROMOLECULAR STRUCTURE ; FAMILY PROTEINS ; MOLECULAR-BASIS ; CHEMICAL-SHIFT ; GROWTH ARREST ; NMR ; IDENTIFICATION ; DOMAIN ; PROGRAM |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000301349400066 |
| 公开日期 | 2015-12-24 |
| 源URL | [http://ir.qibebt.ac.cn/handle/337004/6060]  |
| 专题 | 青岛生物能源与过程研究所_代谢物组学团队 |
| 作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Beijing Normal Univ, Dept Biochem & Mol Biol, Beijing 100875, Peoples R China 3.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Qingdao 266101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Gong, Weibin,Zhou, Tao,Mo, Jinjin,et al. Structural Insight into Recognition of Methylated Histone Tails by Retinoblastoma-binding Protein 1[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2012,287(11):8531-8540. |
| APA | Gong, Weibin,Zhou, Tao,Mo, Jinjin,Perrett, Sarah,Wang, Jinfeng,&Feng, Yingang.(2012).Structural Insight into Recognition of Methylated Histone Tails by Retinoblastoma-binding Protein 1.JOURNAL OF BIOLOGICAL CHEMISTRY,287(11),8531-8540. |
| MLA | Gong, Weibin,et al."Structural Insight into Recognition of Methylated Histone Tails by Retinoblastoma-binding Protein 1".JOURNAL OF BIOLOGICAL CHEMISTRY 287.11(2012):8531-8540. |
入库方式： OAI收割
来源：青岛生物能源与过程研究所
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