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Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1 | |
2012 | |
发表期刊 | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA |
ISSN | 0027-8424 |
卷号 | 109期号:44页码:17954-17959 |
发表状态 | 已发表 |
DOI | 10.1073/pnas.1208517109 |
摘要 | Recognition of methylated histone tail lysine residues by tudor domains plays important roles in epigenetic control of gene expression and DNA damage response. Previous studies revealed the binding of methyllysine in a cage of aromatic residues, but the molecular mechanism by which the sequence specificity for surrounding histone tail residues is achieved remains poorly understood. In the crystal structure of a trimethylated histone H3 lysine 4 (H3K4) peptide bound to the tudor-like domains of Spindlin1 presented here, an atypical mode of methyllysine recognition by an aromatic pocket of Spindlin1 is observed. Furthermore, the histone sequence is recognized in a distinct manner involving the amino terminus and a pair of arginine residues of histone H3, and disruption of the binding impaired stimulation of pre-RNA expression by Spindlin1. Our analysis demonstrates considerable diversities of methyllysine recognition and sequence-specific binding of histone tails by tudor domains, and the revelation furthers the understanding of tudor domain proteins in deciphering epigenetic marks on histone tails. |
关键词 | methylation rRNA expression |
URL | 查看原文 |
收录类别 | SCI |
WOS研究方向 | Science & Technology - Other Topics |
WOS类目 | Multidisciplinary Sciences |
WOS记录号 | WOS:000311149900059 |
出版者 | NATL ACAD SCIENCES |
WOS关键词 | STRUCTURAL BASIS ; EXPRESSION ; SMN |
原始文献类型 | Article |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/119813 |
专题 | 个人在本单位外知识产出 |
通讯作者 | Yang, Na; Zhu, Bing; Xu, Rui-Ming |
作者单位 | 1.Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China 2.Natl Inst Biol Sci, Beijing 102206, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 4.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China |
推荐引用方式 GB/T 7714 | Yang, Na,Wang, Weixiang,Wang, Yan,et al. Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2012,109(44):17954-17959. |
APA | Yang, Na.,Wang, Weixiang.,Wang, Yan.,Wang, Mingzhu.,Zhao, Qiang.,...&Xu, Rui-Ming.(2012).Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,109(44),17954-17959. |
MLA | Yang, Na,et al."Distinct mode of methylated lysine-4 of histone H3 recognition by tandem tudor-like domains of Spindlin1".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 109.44(2012):17954-17959. |
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