Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation
文献类型:期刊论文
| 作者 | Bian, CB; Xu, C; Ruan, JB; Lee, KK; Burke, TL; Tempel, W; Barsyte, D; Li, J; Wu, MH; Zhou, BO |
| 刊名 | EMBO JOURNAL
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| 出版日期 | 2011 |
| 卷号 | 30期号:14页码:2829-2842 |
| 关键词 | H3K4 methylation SAGA Sgf29 Tudor |
| 通讯作者 | Workman, JL (reprint author), Stowers Inst Med Res, 1000 E 50th St, Kansas City, MO 64110 USA.,jlw@stowers.org ; zangjy@ustc.edu.cn ; jr.min@utoronto.ca |
| 英文摘要 | The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex is an important chromatin modifying complex that can both acetylate and deubiquitinate histones. Sgf29 is a novel component of the SAGA complex. Here, we report the crystal structures of the tandem Tudor domains of Saccharomyces cerevisiae and human Sgf29 and their complexes with H3K4me2 and H3K4me3 peptides, respectively, and show that Sgf29 selectively binds H3K4me2/3 marks. Our crystal structures reveal that Sgf29 harbours unique tandem Tudor domains in its C-terminus. The tandem Tudor domains in Sgf29 tightly pack against each other face-to-face with each Tudor domain harbouring a negatively charged pocket accommodating the first residue alanine and methylated K4 residue of histone H3, respectively. The H3A1 and K4me3 binding pockets and the limited binding cleft length between these two binding pockets are the structural determinants in conferring the ability of Sgf29 to selectively recognize H3K4me2/3. Our in vitro and in vivo functional assays show that Sgf29 recognizes methylated H3K4 to recruit the SAGA complex to its targets sites and mediates histone H3 acetylation, underscoring the importance of Sgf29 in gene regulation. The EMBO Journal ( 2011) 30, 2829-2842. doi: 10.1038/emboj.2011.193; Published online 17 June 2011 |
| 学科主题 | Biochemistry & Molecular Biology; Cell Biology |
| 类目[WOS] | Biochemistry & Molecular Biology ; Cell Biology |
| 关键词[WOS] | PROTEIN IDENTIFICATION TECHNOLOGY ; STRUCTURAL BASIS ; SACCHAROMYCES-CEREVISIAE ; TUDOR DOMAIN ; ACETYLTRANSFERASE COMPLEXES ; MOLECULAR REPLACEMENT ; COACTIVATOR COMPLEX ; MASS-SPECTROMETRY ; CODING REGIONS ; SWIRM DOMAIN |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000293970100010 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/875] ![]() |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Bian, CB,Xu, C,Ruan, JB,et al. Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation[J]. EMBO JOURNAL,2011,30(14):2829-2842. |
| APA | Bian, CB.,Xu, C.,Ruan, JB.,Lee, KK.,Burke, TL.,...&Min, JR.(2011).Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.EMBO JOURNAL,30(14),2829-2842. |
| MLA | Bian, CB,et al."Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation".EMBO JOURNAL 30.14(2011):2829-2842. |
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