Histone H4 Tails in Nucleosomes: a Fuzzy Interaction with DNA.

ABSTRACT: The interaction of positively charged N-terminal histone tails with nucleosomal DNA plays an important role in chromatin assembly and regulation, modulating their susceptibility to post-translational modifications and recognition by chromatin-binding proteins. Here, we report residue-specific ¹⁵ N NMR relaxation rates for histone H4 tails in reconstituted nucleosomes. These data indicate that H4 tails are strongly dynamically disordered, albeit with reduced conformational flexibility compared to a free peptide with the same sequence. Remarkably, the NMR observables were successfully reproduced in a 2-μs MD trajectory of the nucleosome. This is an important step toward resolving an apparent inconsistency where prior simulations were generally at odds with experimental evidence on

SUBMITTER: Rabdano SO 

PROVIDER: S-EPMC7994933 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature