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

SUBMITTER: Xiang S 

PROVIDER: S-EPMC5947581 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature