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首页> 外文期刊>Journal of Molecular Biology >YEATS Domain-A Histone Acylation Reader in Health and Disease
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YEATS Domain-A Histone Acylation Reader in Health and Disease

机译:Yeats结构域 - 健康和疾病中的组蛋白酰化读者

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摘要

Histone post-translational modifications (PTMs) carry an epigenetic layer of message to regulate diverse cellular processes at the chromatin level. Many of these PTMs are selectively recognized by dedicated effector proteins for normal cell growth and development, while dysregulation of these recognition events is often implicated in human diseases, notably cancer. Thus, it is fundamentally important to elucidate the regulatory mechanism(s) underlying the readout of PTMs on histones. The Yaf9, ENL, AF9, Taf14, Sas5 (YEATS) domain is an emerging reader module that selectively recognizes histone lysine acylation with a preference for crotonylation over acetylation. In the review, we discuss the recognition of histone acylations by the YEATS domain and the biological significance of this readout from multiple perspectives. (C) 2017 Elsevier Ltd. All rights reserved.
机译:组蛋白翻译后修饰(PTMS)携带表观遗传层,以调节染色质水平的不同细胞过程。 这些PTM中的许多是由专用的效应蛋白选择性地识别用于正常细胞生长和发育,而这些识别事件的失调常将涉及人类疾病,特别是癌症。 因此,阐明在组蛋白的PTMS读数下面的监管机制是根本的。 YAF9,EL,AF9,TAF14,SAS5(YEATS)结构域是一种新兴读取器模块,其选择性地识别组蛋白酰基酰化,优选在乙酰化上进行克拉托蛋白化。 在审查中,我们讨论了叶片结构域的组蛋白酰化的识别和从多个视角来的读出的生物学意义。 (c)2017 Elsevier Ltd.保留所有权利。

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