The Dynamic Influence of Linker Histone Saturation within the Poly-Nucleosome Array.

ABSTRACT: Linker histones bind to nucleosomes and modify chromatin structure and dynamics as a means of epigenetic regulation. Biophysical studies have shown that chromatin fibers can adopt a plethora of conformations with varying levels of compaction. Linker histone condensation, and its specific binding disposition, has been associated with directly tuning this ensemble of states. However, the atomistic dynamics and quantification of this mechanism remains poorly understood. Here, we present molecular dynamics simulations of octa-nucleosome arrays, based on a cryo-EM structure of the 30-nm chromatin fiber, with and without the globular domains of the H1 linker histone to determine how they influence fiber structures and dynamics. Results show that when bound, linker histones inhibit DNA flexibilit

SUBMITTER: Woods DC 

PROVIDER: S-EPMC8085065 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature