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Site‐Specific Studies of Nucleosome Interactions by Solid‐State NMR Spectroscopy
Author(s) -
Xiang ShengQi,
le Paige Ulric B.,
Horn Velten,
Houben Klaartje,
Baldus Marc,
van Ingen Hugo
Publication year - 2018
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201713158
Subject(s) - nucleosome , chromatin , histone , nuclear magnetic resonance spectroscopy , chemistry , biophysics , epigenetics , histone code , computational biology , biology , dna , biochemistry , stereochemistry , gene
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.