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Site‐Specific Studies of Nucleosome Interactions by Solid‐State NMR Spectroscopy
Angewandte Chemie International Edition ( IF 16.6 ) Pub Date : 2018-03-13 , DOI: 10.1002/anie.201713158
ShengQi Xiang 1 , Ulric B le Paige 2, 3 , Velten Horn 2, 3 , Klaartje Houben 1, 4 , Marc Baldus 1 , Hugo van Ingen 2, 3
Affiliation  

Chromatin function depends on a dense network of interactions between nucleosomes and a wide range of proteins. A detailed description of these protein–nucleosome interactions is required to reach a full molecular understanding of chromatin function in both genetics and epigenetics. Herein, we show that the structure, dynamics, and interactions of nucleosomes can be interrogated in a residue‐specific manner by using state‐of‐the‐art solid‐state NMR spectroscopy. Using sedimented nucleosomes, high‐resolution spectra were obtained for both flexible histone tails and the non‐mobile histone core. Through co‐sedimentation of a nucleosome‐binding peptide, we demonstrate that protein‐binding sites on the nucleosome surface can be determined. We believe that this approach holds great promise as it is generally applicable, extendable to include the structure and dynamics of the bound proteins, and scalable to interactions of proteins with higher‐order chromatin structures, including isolated and cellular chromatin.

中文翻译:

通过固态核磁共振波谱进行核小体相互作用的位点特异性研究

染色质功能取决于核小体和多种蛋白质之间相互作用的密集网络。需要对这些蛋白质-核小体相互作用进行详细描述,才能对遗传学和表观遗传学中的染色质功能进行全面的分子理解。在此,我们表明,可以通过使用最先进的固态核磁共振波谱以残基特异性方式询问核小体的结构、动力学和相互作用。使用沉积的核小体,获得了柔性组蛋白尾部和非移动组蛋白核心的高分辨率光谱。通过核小体结合肽的共沉淀,我们证明可以确定核小体表面上的蛋白质结合位点。我们相信这种方法具有广阔的前景,因为它具有普遍适用性,可扩展至包括结合蛋白质的结构和动力学,并且可扩展至蛋白质与高级染色质结构(包括分离的和细胞染色质)的相互作用。
更新日期:2018-03-13
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