2016-Sustainable Industrial Processing Summit
SIPS 2016 Volume 7: Yang Intl. Symp. / Multiscale Material Mechanics

Editors:Kongoli F, Aifantis E, Wang H, Zhu T
Publisher:Flogen Star OUTREACH
Publication Year:2016
Pages:190 pages
ISSN:2291-1227 (Metals and Materials Processing in a Clean Environment Series)
CD shopping page

    Molecular dynamics simulations on nucleosome

    Zhenhai Li1;
    1, Kizugawa, Japan;
    Type of Paper: Regular
    Id Paper: 274
    Topic: 1


    The eukaryotic genome is stored as a protein–DNA complex, the nucleosome, which is composed of H3, H4, H2A, and H4 histone proteins. The histone tails, variants of histones, the post-translational modifications on histone tails, and other DNA binding proteins have been shown to regulate nucleosome dynamics, which plays a critical role in gene expression. However, the regulation mechanism is still unclear on a molecular level. Here we present through computational studies on a single nucleosome particle and the particle with certain histone tail truncated. Our simulation unraveled the distinct function of H2A and H3 tails in stabilizing the nucleosome in the closed conformation: the H2A C-terminal tail switches linker DNA opening and closing simply by binding to DNA at different locations, whereas the H3 N-terminal tail regulates linker DNA by binding with a different pattern. Finally, we propose a model illustrating the mechanism by which H3 N-terminal and H2A C-terminal tails regulate nucleosome stability and dynamics.


    Dynamics; Nanoscale; Polymer; Scientific;

    Cite this article as:

    Li Z. Molecular dynamics simulations on nucleosome. In: Kongoli F, Aifantis E, Wang H, Zhu T, editors. Sustainable Industrial Processing Summit SIPS 2016 Volume 7: Yang Intl. Symp. / Multiscale Material Mechanics. Volume 7. Montreal(Canada): FLOGEN Star Outreach. 2016. p. 123-124.