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

Angewandte Chemie
ShengQi XiangHugo van Ingen

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.

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Citations

Jun 16, 2018·Angewandte Chemie·Xiangyan ShiLars Nordenskiöld
Jan 8, 2020·Biomolecular NMR Assignments·Xiangyan ShiLars Nordenskiöld
Apr 17, 2019·Nature Communications·Velten HornHugo van Ingen
Dec 12, 2018·Nature Structural & Molecular Biology·Keda ZhouKarolin Luger
Mar 11, 2020·Frontiers in Molecular Biosciences·Thomas WiegandAnja Böckmann
Jun 14, 2020·International Journal of Molecular Sciences·Balázs Zoltán Zsidó, Csaba Hetényi
Feb 2, 2021·Angewandte Chemie·Sevastyan O RabdanoChristopher P Jaroniec
May 31, 2020·Progress in Nuclear Magnetic Resonance Spectroscopy·Thomas Wiegand
Jun 30, 2021·The Journal of Physical Chemistry Letters·Mohamad ZandianChristopher P Jaroniec
Oct 26, 2021·Chemical Reviews·Alexander A ShcherbakovMei Hong

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Methods Mentioned

BETA
NMR

Software Mentioned

HADDOCK
TALOS

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