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Structure and Dynamics in the Nucleosome Revealed by Solid-State NMR.
Xiangyan Shi1, Chinmayi Prasanna2, Toshio Nagashima3
1School of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, Singapore, 637371, Singapore.
Angewandte Chemie (International Ed. in English)
|June 16, 2018
Summary
Solid-state NMR reveals human histone H4 (hH4) dynamics within nucleosomes. This chromatin protein exhibits flexibility crucial for DNA accessibility and genomic regulation.
Area of Science:
- Molecular Biology
- Biophysics
- Structural Biology
Background:
- Eukaryotic chromatin structure and dynamics are critical for gene regulation.
- Understanding histone protein dynamics provides insights into genomic accessibility.
Purpose of the Study:
- To determine the secondary structure and intramolecular dynamics of human histone H4 (hH4).
- To investigate hH4 structure and dynamics in both nucleosome core particles (NCPs) and nucleosome arrays.
Main Methods:
- Solid-state Nuclear Magnetic Resonance (SSNMR) spectroscopy was employed.
- Analysis focused on hH4 within Mg2+-precipitated NCPs and nucleosome arrays.
Main Results:
- Localized secondary structure elements of hH4 within NCPs.
- Elucidated nanosecond-to-millisecond timescale dynamics, revealing diverse internal motions.
- Identified increased flexibility in regions regulating chromatin mobility and DNA accessibility.
Conclusions:
- hH4 in nucleosome arrays shares structural and dynamic properties with hH4 in NCPs.
- Specific regions (N-terminus, Loop 1, α3 helix) show restricted motion in nucleosome arrays.
- Histone H4 flexibility is integral to chromatin function and genomic regulation.
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