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Structure and Dynamics in the Nucleosome Revealed by Solid‐State NMR
Author(s) -
Shi Xiangyan,
Prasanna Chinmayi,
Nagashima Toshio,
Yamazaki Toshio,
Pervushin Konstantin,
Nordenskiöld Lars
Publication year - 2018
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201804707
Subject(s) - nucleosome , microsecond , chromatin , chromatosome , chemistry , molecular dynamics , intramolecular force , biophysics , histone , linker dna , solid state nuclear magnetic resonance , nanosecond , crystallography , dna , chemical physics , stereochemistry , physics , computational chemistry , nuclear magnetic resonance , biology , biochemistry , laser , astronomy , optics
Eukaryotic chromatin structure and dynamics play key roles in genomic regulation. In the current study, the secondary structure and intramolecular dynamics of human histone H4 (hH4) in the nucleosome core particle (NCP) and in a nucleosome array are determined by solid‐state NMR (SSNMR). Secondary structure elements are successfully localized in the hH4 in the NCP precipitated with Mg 2+ . In particular, dynamics on nanosecond to microsecond and microsecond to millisecond timescales are elucidated, revealing diverse internal motions in the hH4 protein. Relatively higher flexibility is observed for residues participating in the regulation of chromatin mobility and DNA accessibility. Furthermore, our study reveals that hH4 in the nucleosome array adopts the same structure and show similar internal dynamics as that in the NCP assembly while exhibiting relatively restricted motions in several regions consisting of residues in the N‐terminus, Loop 1, and the α3 helix region.