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A Nucleosome Bridging Mechanism for Activation of a Maintenance DNA Methyltransferase.一个核小体桥接机制,用于激活维持 DNA 甲基转移酶。
Mol Cell. 2019 Jan 3;73(1):73-83.e6. doi: 10.1016/j.molcel.2018.10.006. Epub 2018 Nov 8.
2
Structural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain.结构视角下 YEATS 结构域的 π-π-π 堆积机制和 DNA 结合活性。
Nat Commun. 2018 Nov 1;9(1):4574. doi: 10.1038/s41467-018-07072-6.
3
Reading More than Histones: The Prevalence of Nucleic Acid Binding among Reader Domains.阅读不止于组蛋白:阅读结构域中核酸结合的普遍性。
Molecules. 2018 Oct 12;23(10):2614. doi: 10.3390/molecules23102614.
4
Single-particle cryo-EM-How did it get here and where will it go.单颗粒 cryo-EM——它是如何到达这里的,以及它将走向何方。
Science. 2018 Aug 31;361(6405):876-880. doi: 10.1126/science.aat4346.
5
Hydrazide Mimics for Protein Lysine Acylation To Assess Nucleosome Dynamics and Deubiquitinase Action.酰腙模拟物用于蛋白质赖氨酸酰化以评估核小体动力学和去泛素化酶作用。
J Am Chem Soc. 2018 Aug 1;140(30):9478-9485. doi: 10.1021/jacs.8b03572. Epub 2018 Jul 24.
6
The conformation of the histone H3 tail inhibits association of the BPTF PHD finger with the nucleosome.组蛋白 H3 尾部的构象抑制了 BPTF PHD 指与核小体的结合。
Elife. 2018 Apr 12;7:e31481. doi: 10.7554/eLife.31481.
7
Synthetic post-translational modification of histones.组蛋白的合成后翻译修饰。
Curr Opin Chem Biol. 2018 Aug;45:35-47. doi: 10.1016/j.cbpa.2018.02.004. Epub 2018 Feb 28.
8
Total Chemical Synthesis of Modified Histones.修饰组蛋白的全化学合成
Front Chem. 2018 Feb 6;6:19. doi: 10.3389/fchem.2018.00019. eCollection 2018.
9
Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes.PRC2 同时与两个功能不同的核小体结合的冷冻电镜结构。
Nat Struct Mol Biol. 2018 Feb;25(2):154-162. doi: 10.1038/s41594-018-0023-y. Epub 2018 Jan 29.
10
Accessibility of the histone H3 tail in the nucleosome for binding of paired readers.核小体组蛋白 H3 尾部结合配对读取器的可达性。
Nat Commun. 2017 Nov 14;8(1):1489. doi: 10.1038/s41467-017-01598-x.

生成修饰核小体的策略:在结构生物学研究中的应用。

Strategies for Generating Modified Nucleosomes: Applications within Structural Biology Studies.

机构信息

Department of Biochemistry , University of Iowa Carver College of Medicine , Iowa City , Iowa 52246 , United States.

Department of Pharmacology , University of Colorado School of Medicine , Aurora , Colorado 80045 , United States.

出版信息

ACS Chem Biol. 2019 Apr 19;14(4):579-586. doi: 10.1021/acschembio.8b01049. Epub 2019 Mar 12.

DOI:10.1021/acschembio.8b01049
PMID:30817115
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6476189/
Abstract

Post-translational modifications on histone proteins play critical roles in the regulation of chromatin structure and all DNA-templated processes. Accumulating evidence suggests that these covalent modifications can directly alter chromatin structure, or they can modulate activities of chromatin-modifying and -remodeling factors. Studying these modifications in the context of the nucleosome, the basic subunit of chromatin, is thus of great interest; however, the generation of specifically modified nucleosomes remains challenging. This is especially problematic for most structural biology approaches in which a large amount of material is often needed. Here we discuss the strategies currently available for generation of these substrates. We in particular focus on novel ideas and discuss challenges in the application to structural biology studies.

摘要

组蛋白上的翻译后修饰在调节染色质结构和所有 DNA 模板过程中起着关键作用。越来越多的证据表明,这些共价修饰可以直接改变染色质结构,或者可以调节染色质修饰和重塑因子的活性。因此,在核小体(染色质的基本亚基)的背景下研究这些修饰具有重要意义;然而,产生特异性修饰的核小体仍然具有挑战性。对于大多数结构生物学方法来说,这是一个特别大的问题,因为这些方法通常需要大量的材料。在这里,我们讨论了目前可用于生成这些底物的策略。我们特别关注新的想法,并讨论了在应用于结构生物学研究中的挑战。