Chemical biology of protein arginine modifications in epigenetic regulation.

Chemical biology of protein arginine modifications in epigenetic regulation.
复制标题

DOI:
10.1021/acs.chemrev.5b00003
复制
发表时间:
2015-06-10
期刊:
影响因子:
62.1
通讯作者:
Thompson, Paul R.
Thompson, Paul R.
中科院分区:
化学1区
文献类型:
--
作者:
Fuhrmann, Jakob;Clancy, Kathleen W.;Thompson, Paul R.

文献摘要

参考文献

被引文献

相似文献

组蛋白的翻译后修饰(PTMs)是表观遗传调控的标志。它们提供了一种调节染色质结构的机制,并构成了所谓的“组蛋白密码”的主要特征。(1)该编码的功能是将外源性和内源性信号整合到一套多样化的组蛋白PTM模式中,从而实现基因表达的表观遗传控制。这一过程的关键调控因子是所谓的“书写者”和“擦除者”,它们通过动态修饰组蛋白和其他染色质相关蛋白,以及“读取者”,它们解释这些ptm,从而促进下游基因表达的激活或抑制。(2)作者是组蛋白修饰酶,可根据其氨基酸底物偏好进行分组,主要影响赖氨酸、精氨酸和丝氨酸残基。(3)这些酶可以根据它们催化的共价修饰的类型进一步分类。组蛋白修饰包括乙酰化、甲基化、磷酸化,以及最近描述的瓜氨酸化、泛素化、sumo化、脯氨酸异构化、o - glcn酰化和adp核糖基化修饰。(1b, 3)在详细的质谱分析的基础上,至少有15种不同类型的共价组蛋白修饰,(4)并且由于组蛋白蛋白在多个位点和不同的化学计量学上被修饰,组蛋白标记的总数为160个。(5)尽管我们对组蛋白修饰如何促进基因转录的表观遗传控制的理解在过去的15年里有了很大的发展,但这大量修饰的确切影响,更不用说它们之间的串扰,还没有完全认识到。
Post-translational modifications (PTMs) of histone proteins are a hallmark of epigenetic regulation. They provide a mechanism to modulate chromatin structure and constitute the main features of the so-called “histone code”.(1) The proposed function of this code is to integrate exogenous and endogenous signals into a diverse set of histone PTM patterns to enable the epigenetic control of gene expression. The key regulators of this process are the so-called “writers” and “erasers”, which act by dynamically modifying histones, and other chromatin-associated proteins, as well as the “readers”, which interpret these PTMs, thereby facilitating the downstream activation or repression of gene expression.(2)The writers are histone-modifying enzymes that can be grouped according to their amino acid substrate preference, affecting mainly lysine, arginine, and serine residues.(3) These enzymes can be further classified according to the type of covalent modification that they catalyze. Histone modifications include acetylation, methylation, phosphorylation, and the more recently described modifications of citrullination, ubiquitination, SUMOylation, proline isomerization, O-GlcNAcylation, and ADP-ribosylation.(1b, 3) On the basis of detailed mass spectrometric analyses, there are at least 15 different types of covalent histone modifications,(4) and since histone proteins are modified at multiple sites, and different stoichiometries, the total number of histone marks is> 160.(5) Although our understanding of how histone modifications contribute to the epigenetic control of gene transcription has grown immensely over the past∼ 15 years, the precise impact of this vast number of modifications, not to mention the crosstalk between them, has yet to be fully realized.
DOI: 10.1002/bip.22127
发表时间: 2013-02
期刊: BIOPOLYMERS
影响因子: 2.9
作者:
Bicker, Kevin L.;Thompson, Paul R.
通讯作者: Thompson, Paul R.
DOI: 10.1016/0003-9861(72)90319-0
发表时间: 1972-01-01
影响因子: 3.9
作者:
BLETHEN, SL
通讯作者: BLETHEN, SL
DOI: 10.1039/jr9510002492
发表时间: 1951-01-01
期刊: JOURNAL OF THE CHEMICAL SOCIETY
影响因子: --
作者:
ANGYAL, SJ;WARBURTON, WK
通讯作者: WARBURTON, WK
新型组蛋白翻译后修饰的蛋白质组学表征。
DOI: 10.1186/1756-8935-6-24
发表时间: 2013-08-01
影响因子: 3.9
作者:
Arnaudo AM;Garcia BA
通讯作者: Garcia BA
DOI: 10.1074/jbc.m115.636894
发表时间: 2015-04-10
影响因子: 4.8
作者:
Burgos, Emmanuel S.;Wilczek, Carola;Shechter, David
通讯作者: Shechter, David