Site‐Specific Studies of Nucleosome Interactions by Solid‐State NMR Spectroscopy

Abstract: 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.

Object Details

• Location: Deutsche Nationalbibliothek Frankfurt am Main
• Extent: Online-Ressource
• Language: Englisch

References and Relationships

• Bibliographic citation: Site‐Specific Studies of Nucleosome Interactions by Solid‐State NMR Spectroscopy ; volume:57 ; number:17 ; year:2018 ; pages:4571-4575 ; extent:5 ; Angewandte Chemie / International edition. International edition ; 57, Heft 17 (2018), 4571-4575 (gesamt 5)

Contributors, Places and Time

• Creator: Xiang, ShengQi ; le Paige, Ulric B. ; Horn, Velten ; Houben, Klaartje ; Baldus, Marc ; van Ingen, Hugo

Further information

• DOI: 10.1002/anie.201713158
• URN: urn:nbn:de:101:1-2022091107182504564113
• Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
• Last update: 15.08.2025, 7:25 AM CEST