Site-Specific Studies of Nucleosome Interactions by Solid-State NMR.
Related Articles Site-Specific Studies of Nucleosome Interactions by Solid-State NMR.
Angew Chem Int Ed Engl. 2018 Feb 21;:
Authors: Xiang S, le Paige UB, Horn V, Houben K, Baldus M, van Ingen H
Abstract
Chromatin function depends on a dense network of interactions between nucleosomes and 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. Here, we show that the structure, dynamics and interactions of nucleosomes can be interrogated in a residue-specific manner using state-of-the-art solid-state NMR. Using sedimented nucleosomes, high-resolution spectra are 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 or cellular chromatin.
PMID: 29465771 [PubMed - as supplied by publisher]
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