4.8 Article

Conformational Dynamics of Histone H3 Tails in Chromatin

Journal

JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 12, Issue 26, Pages 6174-6181

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.1c01187

Keywords

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Funding

  1. National Institutes of Health [R01GM118664, R01GM123743, S10OD012303]
  2. National Science Foundation [MCB-1715174]

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In this study, high-resolution NMR measurements were used to investigate the dynamics and interactions of H3 tails in nucleosome arrays with different lengths of linker DNA. The H3 tail dynamics in nucleosome arrays were found to be significantly attenuated compared to nucleosomes with or without linker DNA, but were not modulated by the specific linker DNA length investigated.
Chromatin is a supramolecular DNA-protein complex that compacts eukaryotic genomes and regulates their accessibility and functions. Dynamically disordered histone H3 N-terminal tails are among key chromatin regulatory components. Here, we used high-resolution-magic-angle-spinning NMR measurements of backbone amide N-15 spin relaxation rates to investigate, with residue-specific detail, the dynamics and interactions of H3 tails in recombinant C-13,N-15-enriched nucleosome arrays containing 15, 30, or 60 bp linker DNA between the nucleosome repeats. These measurements were compared to analogous data available for mononucleosomes devoid of linker DNA or containing two 20 bp DNA overhangs. The H3 tail dynamics in nucleosome arrays were found to be considerably attenuated compared with nucleosomes with or without linker DNA due to transient electrostatic interactions with the linker DNA segments and the structured chromatin environment. Remarkably, however, the H3 tail dynamics were not modulated by the specific linker DNA length within the 15-60 bp range investigated here.

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