ArticleMagnetic resonance (Gottingen, Germany)2021
Characterization of nucleosome sediments for protein interaction studies by solid-state NMR spectroscopy.
Article in Magnetic resonance (Gottingen, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- Structural and dynamic studies of chromatin by solid-state NMR spectroscopy.Current opinion in structural biology · 2024Review
- Unveiling structural and dynamical features of chromatin using NMR spectroscopy.Magnetic resonance letters · 2024Review
- Studying large biomolecules as sedimented solutes with solid-state NMR.Biophysics reports · 2024Article
- Initial Primer Synthesis of a DNA Primase Monitored by Real-Time NMR Spectroscopy.Journal of the American Chemical Society · 2024Article
- Structural and dynamical investigation of histone H2B in well-hydrated nucleosome core particles by solid-state NMR.Communications biology · 2023Article
- Epitope Mapping and Binding Assessment by Solid-State NMR Provide a Way for the Development of Biologics under the Quality by Design Paradigm.Journal of the American Chemical Society · 2022Article
- Histone H3 core domain in chromatin with different DNA linker lengths studied byFrontiers in molecular biosciences · 2022Article
- Recent Advances in Investigating Functional Dynamics of Chromatin.Frontiers in genetics · 2022Review
- Evaluation of the Higher Order Structure of Biotherapeutics Embedded in Hydrogels for Bioprinting and Drug Release.Analytical chemistry · 2021Article
- Emerging Contributions of Solid-State NMR Spectroscopy to Chromatin Structural Biology.Frontiers in molecular biosciences · 2021Review
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Regulation of DNA-templated processes such as gene transcription and DNA repair depend on the interaction of a wide range of proteins with the nucleosome, the fundamental building block of chromatin. Both solution and solid-state NMR spectroscopy have become an attractive approach to study the dynamics and interactions of nucleosomes, despite their high molecular weight of ~ 200 kDa. For solid-state NMR (ssNMR) studies, dilute solutions of nucleosomes are converted to a dense phase by sedimentation or precipitation. Since nucleosomes are known to self-associate, these dense phases may induce extensive interactions between nucleosomes, which could interfere with protein-binding studies. Here, we characterized the packing of nucleosomes in the dense phase created by sedimentation using NMR and small-angle X-ray scattering (SAXS) experiments. We found that nucleosome sediments are gels with variable degrees of solidity, have nucleosome concentration close to that found in crystals, and are stable for weeks under high-speed magic angle spinning (MAS). Furthermore, SAXS data recorded on recovered sediments indicate that there is no pronounced long-range ordering of nucleosomes in the sediment. Finally, we show that the sedimentation approach can also be used to study low-affinity protein interactions with the nucleosome. Together, our results give new insights into the sample characteristics of nucleosome sediments for ssNMR studies and illustrate the broad applicability of sedimentation-based NMR studies.
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