Tudor: a versatile family of histone methylation 'readers'.

Tudor: a versatile family of histone methylation 'readers'.
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DOI:
10.1016/j.tibs.2013.08.002
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发表时间:
2013-11
影响因子:
13.8
通讯作者:
Wang, Gang Greg
Wang, Gang Greg
中科院分区:
生物学1区
文献类型:
--
作者:
Lu, Rui;Wang, Gang Greg

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Tudor结构域包含介导各种DNA模板化生物过程所需的蛋白质-蛋白质相互作用的基序家族。新出现的证据证明了Tudor家族结构域的多功能性,通过鉴定它们与各种各样的组蛋白甲基化标记的特异性相互作用。在此,我们讨论了一些Tudor蛋白(包括JMJD 2A,53 BP 1,SGF 29,Spindlin 1,UHRF 1,PHF 1,PHF 19和SHH 1)在“阅读”独特的甲基化事件中的新功能,以促进DNA损伤修复或调节转录。这篇综述涵盖了我们最近对组蛋白-Tudor相互作用的分子基础及其生物学结果的理解。由于含有Tudor的蛋白质的失调与某些人类疾病相关,因此Tudor相互作用的药理学靶向可以为治疗干预提供新的途径。
The Tudor domain comprises a family of motifs that mediate protein-protein interactions required for various DNA-templated biological processes. Emerging evidence demonstrates a versatility of the Tudor family domains by identifying their specific interactions to a wide variety of histone methylation marks. Here, we discuss novel functions of a number of Tudor-containing proteins (including JMJD2A, 53BP1, SGF29, Spindlin1, UHRF1, PHF1, PHF19 and SHH1) in ‘reading’ unique methylation events on histones in order to facilitate DNA damage repair or regulate transcription. This review covers our recent understanding of the molecular bases for histone-Tudor interactions and their biological outcomes. As deregulation of Tudor-containing proteins is associated with certain human disorders, pharmacological targeting of Tudor interactions could provide new avenues for therapeutic intervention.
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